Phosphorylated IRAK2, like its paralog IRAK1, possibly dissociates from the activated receptor as shown here, although mechanism of IRAK2 activation by IRAK4 followed by TRAF6 binding remains to be deciphered.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9NWZ3-1", "Q06187-1", "Q9Y4K3-1", "P51617-1" ], "evidence": [ { "id": "R-HSA-166362", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-166362" } ] }, { "id": "R-HSA-166363", "name": "TRAF6 binds to hp- IRAK1", "equation": "", "summary": "Hyperphosphorylated IRAK1, still within the receptor complex, binds TRAF6 through multiple regions including the death domain, the undefined domain and the C-terminal C1 domain (Li et al. 2001). The C-terminal region of IRAK-1 contains three potential TRAF6-binding sites; mutation of the amino acids (Glu544, Glu587, Glu706) in these sites to alanine greatly reduces activation of NFkappaB (Ye et al. 2002).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9NWZ3-1", "Q06187-1", "Q9Y4K3-1", "P51617-1" ], "evidence": [ { "id": "R-HSA-166363", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-166363" } ] }, { "id": "R-HSA-2197698", "name": "Src phosphorylate WASP,N-WASP", "equation": "", "summary": "WASP is phosphorylated on Tyr291 (Cory et al. 2002) and N-WASP (WASL) on Tyr256 (Wu et al. 2004) by Src family of tyrosine kinases and this phosphorylation may release the autoinhibitory intramolecular interactions. The phosphorylation seems to be enhanced by the activation of CDC42. WASP phosphorylation and binding of CDC42 have a synergistic effect on the activation of the ARP2/3 complex (Takenawa & Suetsugu 2007). In N-WASP, the phosphorylation may reduce its nuclear translocation and may sustain it in its functional site in the cytoplasm (Wu et al. 2004).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1", "P60953-2", "Q05397-1" ], "evidence": [ { "id": "R-HSA-2197698", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2197698" } ] }, { "id": "R-HSA-2201322", "name": "TIRAP is phosphorylated by BTK", "equation": "", "summary": "Upon activation of TLR2/or 4 signaling pathway TIRAP(MAL), a TIR domain\u2013containing adapter protein, undergoes tyrosine phosphorylation (Piao W et al. 2008; Gray P et al. 2006). Bruton's tyrosine kinase (BTK) was shown to mediate the TIRAP phosphorylation (Jefferies CA et al. 2003; Gray P et al. 2006). BTK-specific inhibitor, LFM-A13, blocked the phosphorylation of TIRAP in human monocytic cell line THP-1 stimulated with LPS or macrophage-activating lipopeptide-2 (MALP-2) (Gray P et al. 2006). LFM-A13 also inhibited activation of NFkappaB in LPS-treated THP-1 (Jefferies CA et al. 2003). Besides BTK kinase TIRAP was shown to associate with other kinases such as protein kinase C delta (PKC delta) suggesting their regulatory role in TIRAP activation (Kubo-Murai M et al. 2007).
Tyr-86, Tyr-106 and Tyr-187 were identified as possible phosphorylation sites (Gray P et al. 2006). An additional study has shown that Tyr-86, Tyr-106, and Tyr-159 are important residues, as mutagenesis of these residues impaired TIRAP (MAL) phosphorylation, affected its interaction with BTK and also impaired downstream signaling (Piao W et al. 2008). BTK-mediated phosphorylation of TIRAP leads to recruitment of suppressor of cytokine signaling 1 (SOCS1), which assembles K48-linked polyubiquitin chains resulting in TIRAP's proteosomal degradation, disrupting the TLR complex, and terminating signaling (Mansell A et al. 2006). TIRAP function is also regulated by the cysteine protease caspase-1, which cleaves the protein in a region of the molecule that interacts with MyD88 and TLR4 (Ulrichts P et al. 2010).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-2201322", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2201322" } ] }, { "id": "R-HSA-2262775", "name": "Dissociation of p-IRAK2:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex", "equation": "", "summary": "Hyperphosphorylated IRAK1 and TRAF6 are thought to dissociate from the activated receptor. (Gottipati et al. 2007) but the IRAK1:TRAF6 complex may remain associated with the membrane (Dong et al. 2006).
Phosphorylated IRAK2, like its paralog IRAK1, possibly dissociates from the activated receptor as shown here, although mechanism of IRAK2 activation by IRAK4 followed by TRAF6 binding remains to be deciphered.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9NWZ3-1",
"Q06187-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-2262775",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2262775"
}
]
},
{
"id": "R-HSA-2262777",
"name": "TRAF6 binds to p-IRAK2",
"equation": "",
"summary": "IRAK-2 has two TRAF6 binding motifs that are responsible for initiating TRAF6 signaling transduction (Ye H et al 2002). IRAK2 point mutants with mutated TRAF6-binding motifs abrogate NFkB activation and are incapable to stimulate TRAF6 ubiquitination (Keating SE et al 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9NWZ3-1",
"Q06187-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-2262777",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2262777"
}
]
},
{
"id": "R-HSA-2424476",
"name": "Activation of RAC1 by VAV2/3",
"equation": "",
"summary": "Activated VAV2/3 act as guanine nucleotide exchange factors (GEFs) for RAC-1, catalysing the exchange of bound GDP for GTP.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P19174-1",
"Q06187-1",
"P63000-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-2424476",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424476"
}
]
},
{
"id": "R-HSA-2424481",
"name": "Recruitment of VAV and BTK to p-SLP-76",
"equation": "",
"summary": "VAV2 and VAV3 are expressed in human NK cells and play a central role in NK cell-mediated cytotoxicity. They are required for DAP12-mediated signaling; their loss profoundly impairs DAP12-induced cytotoxicity (Billadeau et al. 2000, Cella et al. 2004). Phosphorylated SLP-76 tyrosines Y113 and Y128 provide binding sites for the SH2 domains of VAV. The binding of VAV to these phosphotyrosine residues may link SLP-76 to the Jun amino-terminal kinase (JNK) pathway and the actin cytoskeleton. Y145 has been implicated in the binding of SLP-76 to the Tec family kinase BTK (Kettner et al. 2003). BTK is required for secretion of pro-inflammatory cytokines, phosphorylation of ERK1/2 and PLCgamma and Ca2+ mobilization (Ormsby et al. 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P19174-1",
"Q06187-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-2424481",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424481"
}
]
},
{
"id": "R-HSA-2424484",
"name": "Phosphorylation of BTK by p-SYK",
"equation": "",
"summary": "In myeloid cells BTK is phosphorylated on Y551 upon DAP12 activation in a SYK kinase-dependent manner. Y551 is located in the activation loop of BTK, known to be required for activation and kinase activity. Y223 in the SH3 domain of BTK is autophosphorylated, which may also be involved in BTK activation (Ormsby et al. 2010, Rawlings et al. 1996).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424484",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424484"
}
]
},
{
"id": "R-HSA-2424485",
"name": "Release of p-PLCG1",
"equation": "",
"summary": "Activated PLC-gamma1 disassociates from LAT. Membrane binding is crucial for PLC-gamma 1 activity. The PH-domain of PLC-gamma 1 binds to phosphatidylinositol 3,4,5-trisphosphate [PdtIns(3,4,5)P3], and is targeted to the membrane (Todderud et al. 1990, Wang & Wang. 2003, Kim et al. 2000). Activated PLCG1 then hydrolyses PIP2 to Inositol 1,4,5-triphosphate (IP3) and DAG",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P19174-1",
"Q06187-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-2424485",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424485"
}
]
},
{
"id": "R-HSA-2424486",
"name": "Phosphorylation and activation of VAV2/VAV3 by SYK",
"equation": "",
"summary": "VAV exists in an auto-inhibitory state, folded in such a way as to inhibit the GEF activity of its DH domain. This folding is mediated through binding of tyrosines in the acidic domain to the DH domain and through binding of the calponin homology (CH) domain to the C1 region. Activation of VAV may involve three events which relieve this auto-inhibition: phosphorylation of tyrosines in the acidic domain causes them to be displaced from the DH domain; binding of a ligand to the CH domain may cause it to release the C1 domain; binding of the PI3K product PIP3 to the PH domain may alter its conformation (Aghazadeh et al. 2000). VAV2/3 are phosphorylated on Y172/Y173 respectively in the acidic domain. This is mediated by SYK and Src-family tyrosine kinases (Deckert et al. 1996, Schuebel et al. 1998). Once activated, VAV2/VAV3 are involved in the activation of RAC1, PAK1, MEK and ERK.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424486",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424486"
}
]
},
{
"id": "R-HSA-2424487",
"name": "Phosphorylation of PLC-gamma by p-BTK/p-SYK",
"equation": "",
"summary": "Three tyrosine residues at positions 771, 783 and 1254 in PLCgamma1 have been identified as the sites of receptor tyrosine kinase phosphorylation. Of these Y783 and Y1254 are required for PLC-gamma1 activation.
In myeloid cells phosphorylation of the tyrosine residues of PLC-gamma1 is mediated by SYK and BTK kinases (Ormsby et al. 2010, Kim et al. 1994, Law et al. 1996, Watanabe et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424487",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424487"
}
]
},
{
"id": "R-HSA-2559414",
"name": "Activated TLR2/4:TIRAP interacts with BTK",
"equation": "",
"summary": "Bruton's tyrosine kinase (BTK) is a cytoplasmic protein tyrosine kinase, which plays an essential role in B cell receptor (BCR) signaling (Brunner C et al. 2005). BTK has been also implicated in TLR signaling (Lee KG et al. 2012, Jefferies CA et al. 2003; Doyle SL et al. 2007). Interaction studies revealed that BTK can associate with intracellular TIR-domains of TLRs 4, 6, 8 and 9. Furthermore, BTK was found to interact with other proteins involved in TLR2/4 signaling - MyD88, MAL and IRAK-1 (Jefferies CA et al. 2003)
Loss of BTK function causes X-linked agammaglobulinemia (XLA), a rare primary immunode?ciency disease with severe defects in early B-cell development resulting in an almost complete absence of peripheral B cells and severely reduced serum levels of immunoglobulins of all classes (V\u00e4liaho J et al. 2006). Affected individuals suffer from recurrent bacterial and enteroviral infections. It remains unclear whether XLA patients have normal or impared TLR signaling functions. LPS-stimulated monocytes from XLA patients were found to produce reduced amounts of TNFalpha (Horwood NJ et al. 2003), These data contradict a study that showed enhanced amounts of TNFalpha and IL6 comparing to control cells, starting at 6 hours and extending for 48 hours (Marron TU et al. 2012). The other group reported similar expression TNFalpha upon TLR4 triggering, compared with healthy control cells (Perez de Diego R et al. 2006). Thus, the effect of BTK deficiency on TLR-mediated inflammation needs to be further clarified.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-2559414", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2559414" } ] }, { "id": "R-HSA-2730833", "name": "Phosphorylation of TEC kinases by p-SYK", "equation": "", "summary": "BTK/ITK are activated in a two step model. In the first step they are recruited to the membrane by binding to PIP3 or, alternatively with other binding partners like SLP-76. Once at the membrane SYK or Src-kinases in the vicinity phosphorylates Y551 (Y512 in ITK) in the activation loop of the catalytic domain of BTK to fully activate it (Rawlings et al. 1996, Park et al. 1996, Kawakami et al. 1994).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P19174-1", "Q06187-1", "P07948-1", "P16885-1", "P43405-1", "P42680-1", "P42681-1", "Q08881-1" ], "evidence": [ { "id": "R-HSA-2730833", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730833" } ] }, { "id": "R-HSA-2730847", "name": "Hydrolysis of PIP2 by PLCG", "equation": "", "summary": "Phosphoinositol 4,5-bisphosphate (PIP2) is cleaved in to two most important second messengers diacylglycerol (DAG) and Inositol 1,4,5-triphosphate (IP3) by phospholipase C (PLC). DAG remains within the membrane and activates protein kinase C (PKC) while IP3 leaves the cell membrane and binds to IP3 receptor that releases Ca2+ from endoplasmic reticulum (ER).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P19174-1", "Q06187-1", "P16885-1", "P42680-1", "P42681-1", "Q08881-1" ], "evidence": [ { "id": "R-HSA-2730847", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730847" } ] }, { "id": "R-HSA-2730858", "name": "Autophosphorylation of BTK/ITK", "equation": "", "summary": "After initial phosphorylation by SFK's, subsequently Y223 (Y180 in ITK and Y206 in TEC) in the SH3 domain of BTK is autophosphorylated, which may prevent inhibitory intramolecular interactions (Nore et al. 2003, Joseph et al. 2007, Park et al. 1996)", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P19174-1", "Q06187-1", "P16885-1", "P42680-1", "P42681-1", "Q08881-1" ], "evidence": [ { "id": "R-HSA-2730858", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730858" } ] }, { "id": "R-HSA-2730885", "name": "Recruitment of TEC kinases to p-SLP-76", "equation": "", "summary": "Mast cells express four out of five Tec family members (i.e. BTK, ITK, RLK and TEC) and are activated upon cross-linking of FCERI. They are recruited to the membrane via the interaction of their PH domain with PtdIns(3,4,5)P3 phosphate and their SH2 domain with Y145 of SLP-76 (Kettner et al. 2003). BTK is more important for early response such as phosphorylation of PLC-gamma2 and Ca2+ mobilization, whereas ITK regulates the late responses such as changes in gene expression and cytokine secretion. BTK deficient mice have mild defects in degranulation and severe impairments in the production of proinflammatory cytokines upon FCERI cross-linking (Hata et al. 1998). ITK deficient mice have been reported to have reduced MC degranulation and responses to allergic asthma (Forssell et al. 2005). However, Bone marrow derived mast cells (BMMC) derived from ITK deficient mice display a normal degranulation response but secrete elevated level of cytokines (TNFa and IL-13) (Iyer & August 2008). TEC kinase is also one of the crucial regulators of murine mast cell function. TEC is phosphorylated and activated upon FCERI stimulation. TEC deficient bone marrow derived mast cells did not show any in vitro or in vivo defects in histamine release. However, the generation of the leukotriene LTC4 was severely impaired in the absence of TEC (Schmidt et al. 2009).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P19174-1", "Q06187-1", "P16885-1", "P42680-1", "P42681-1", "Q08881-1" ], "evidence": [ { "id": "R-HSA-2730885", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730885" } ] }, { "id": "R-HSA-2730888", "name": "Phosphorylation of PLC-gamma", "equation": "", "summary": "Tyrosine phosphorylation of PLC-gamma enhances its catalytic activity. BTK and SYK are involved in the phosphorylation of PLC-gamma (PLCG). Phosphorylation of tyrosine residues 753, 759, 1197, and 1217 in PLCG2 and 771, 783, and 1254 in PLCG1 have been identified as BTK/SYK-dependent phosphorylation sites.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P19174-1", "Q06187-1", "P07948-1", "P16885-1", "P43405-1", "P42680-1", "P42681-1", "Q08881-1" ], "evidence": [ { "id": "R-HSA-2730888", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730888" } ] }, { "id": "R-HSA-5602353", "name": "Defective IRAK4 variants do not bind MyD88:MAL:BTK:activated TLR2/4", "equation": "", "summary": "Patients with an autosomal recessive form of IRAK4 deficiency bear homozygous or compound heterozygous mutations in the IRAK4 gene, that result in increased susceptibility to pyogenic bacterial infections in early childhood (Picard C et al. 2010; Picard C et al. 2011). Most of the mutations are nonsense or frame shift, that create premature stop codons leading to abolished IRAK4 production (Picard C et al. 2003; Ku CL et al. 2007; Yamamoto T et al. 2014). Here we describe two nonsense mutations that have been shown to compromise TLR2 and TLR4 signaling in response to their agonists Pam3CSK4 (TLR1/2), Pam2CSK4 (TLR2/6) and LPS (TLR4) (Ku CL et al. 2007).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9NWZ3-1", "Q06187-1" ], "evidence": [ { "id": "R-HSA-5602353", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5602353" } ] }, { "id": "R-HSA-5602383", "name": "Defective MyD88 does not oligomerize within the activated TLR2/4 complex", "equation": "", "summary": "All TLRs, except for TLR3, employ the MyD88-dependent signaling pathway. Autosomal recessive MyD88 deficiency predispose affected patients to recurrent pyogenic bacterial infection due to abolished TLR-mediated cytokine responses of the blood cells (von Bernuth H et al. 2008; Currie AJ et al. 2004). Here we describe several natural loss-of-function MyD88 variants (E52del, L93P, E65del, S34T) that showed severely reduced NFkB activation in human cell-based assays due to reduced homooligomerization and IRAK4 interaction, the two crucial events in the assembly of the Myddosome complex (George J et al. 2011; Nagpal K et al. 2011; Yamamoto T et al. 2014).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-5602383", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5602383" } ] }, { "id": "R-HSA-5602606", "name": "Defective MyD88 does not bind MAL(TIRAP):TLR2/4", "equation": "", "summary": "The sorting MyD88 adaprtor-like (MAL or TIRAP) normally recruits MyD88 to activated TLR2 and TLR4 receptor complexes (Horng T et al. 2002; Verstak B et al. 2009). MyD88 interacts with MAL (TIRAP) via their TIR domains and activates a downstream signaling pathway mediated by TLR2 and TLR4 (Ohnishi H et al. 2009). A GST pull-down assay showed that defective MyD88 R196C variant loses its ability to bind to MAL (Yamamoto T et al. 2014).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-5602606", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5602606" } ] }, { "id": "R-HSA-5602672", "name": "Defective IRAK4 does not bind MyD88 within the TLR2/4 complex", "equation": "", "summary": "Autosomal recessive IRAK-4 deficiency leads to impaired TLR responses in leukocytes and is associated with increased susceptibility to pyogenic bacterial infections in childhood (Picard C et al. 2003; Medvedev AE et al. 2003; Yamamoto T et al. 2014). Unlike most of the identified gene variants of IRAK4 with nonsense or frame shift mutations that create premature stop codons and result in abolished IRAK4 production, the protein level of missence variant IRAK4 R12C was comparable with wild type (WT) when expressed in human embryonic kidney 293 (HEK293T) cells (Ku CL et al. 2007; Yamamoto T et al. 2014). Analytical gel filtration of recombinant WT or mutant IRAK4 and MyD88 proteins revealed that IRAK4 R12C failed to form a complex with MyD88. These results are in agreement with nuclear magnetic resonance (NMR) titration study that showed a lower affinity of IRAK R12C variant towards 1H-15N-labeled MyD88 N-terminal domain (Yamamoto T et al. 2014).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9NWZ3-1", "Q06187-1" ], "evidence": [ { "id": "R-HSA-5602672", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5602672" } ] }, { "id": "R-HSA-8863895", "name": "IKKB phosphorylates SNAP23", "equation": "", "summary": "A major reserve of MHC-I in dendritic cells reside within the endocytic recycling compartments (ERC). MHC-I trafficking to the ERC is regulated by the activity of Rab11a and subsequent trafficking from ERC to phagosomes is controlled by TLR-MyD88-IKK2-dependent phosphorylation of phagosomal SNAP23. Toll-like receptor (TLR) signalling regulate cross-presentation as they regulate phagocytosis and phagolysosomal fusion (Nair et al. 2011). MHC-I bearing ERC are enriched with R-SNAREs like RAB11a, VAMP3, and VAMP8. These SNARE molecules can interact with Q-SNARE SNAP23 present on phagosomes and this mediates membrane fusion. This interaction of SNAP23 with R-SNAREs require phosphorylation of SNAP23 (on Ser-95) by IKK2, and IKK2 is activated by TLR signalling. SNAP23 phosphorylation may increase SNAP23 binding to SNAREs. It may also regulate platelet and mast cell secretion (Karim et al. 2013, Suziki & Verma 2008).", "cellular_location": "cytosol, phagocytic vesicle membrane", "input_participant_list": [ "R-HSA-8863966" ], "output_participant_list": [ "R-HSA-8863923" ], "enzyme_list": [ "Q06187-1", "O15111-1", "O14920-1" ], "evidence": [ { "id": "R-HSA-8863895", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8863895" } ] }, { "id": "R-HSA-8964241", "name": "G beta-gamma complex and PIP3 recruit BTK to membrane", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G-proteins) that have alpha, beta and gamma subunits. Upon activation, the alpha subunit of G-proteins dissociates from beta-gamma and the both are then free to regulate downstream effectors. G-protein beta-gamma complex, along with phosphatidylinositol 3,4,5-trisphosphate (PIP3), recruits the non-receptor Tyrosine-protein kinase BTK to the cell membrane. This recruitment involves binding of the G-protein beta-gamma complex to the pleckstrin homology/Tec-homology module of Btk. Here, BTK is activated and subsequently released to the cytoplasm. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964241", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964241" } ] }, { "id": "R-HSA-8964246", "name": "BTK in G alpha (12)-BTK complex is activated", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein subunit alpha-12 (GNA12) can bind the non-receptor Tyrosine-protein kinase BTK. In this complex, GNA12 triggers BTK activation. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964246", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964246" } ] }, { "id": "R-HSA-8964271", "name": "BTK in PIP3:BTK:G beta-gamma complex is activated", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G-proteins) that have alpha, beta and gamma subunits. Upon activation, the alpha subunit of G-proteins dissociates from beta-gamma and the both are then free to regulate downstream effectors. G-protein beta-gamma complex, along with phosphatidylinositol 3,4,5-trisphosphate (PIP3), recruits the non-receptor Tyrosine-protein kinase BTK to the cell membrane. In the membrane, the G-protein beta-gamma complex binds to the catalytic domain of BTK and activates it. Active BTK is then released to the cytoplasm. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964271", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964271" } ] }, { "id": "R-HSA-8964274", "name": "G alpha (12) binds BTK", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein subunit alpha-12 (GNA12) can bind directly to the PH domain of the non-receptor Tyrosine-protein kinase BTK (BTK) in vitro and in vivo. This binding results in the activation of BTK. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964274", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964274" } ] }, { "id": "R-HSA-8964280", "name": "Active Gq binds BTK", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind directly to the THSH3 domain of the non-receptor Tyrosine-protein kinase BTK in vitro and in vivo. This binding results in a conformational change in BTK, which leads to its activation. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964280", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964280" } ] }, { "id": "R-HSA-8964284", "name": "BTK in active Gq-BTK complex is activated", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind directly to the non-receptor Tyrosine-protein kinase BTK. This binding breaks intramolecular interactions in BTK thereby making the kinase domain available for substrates. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964284", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964284" } ] }, { "id": "R-HSA-8964317", "name": "PIP3:BTK:G beta-gamma complex dissociates to Active BTK, PIP3 and G beta-gamma complex", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G-proteins) that have alpha, beta and gamma subunits. Upon activation, the alpha subunit of G-proteins dissociates from beta-gamma and the both are then free to regulate downstream effectors. G-protein beta-gamma complex, along with phosphatidylinositol 3,4,5-trisphosphate (PIP3), recruits the non-receptor Tyrosine-protein kinase BTK to the cell membrane. Here, the G-protein beta-gamma complex activates BTK. Once active, BTK dissociates from PIP3 and G-protein beta-gamma complex and is released to the cytoplasm to phosphorylate downstream substrates. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964317", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964317" } ] }, { "id": "R-HSA-8964333", "name": "G alpha (12)-BTK complex dissociates to Active BTK and G alpha (12)", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein subunit alpha-12 (GNA12) can bind to the non-receptor Tyrosine-protein kinase BTK. This complex facilitates BTK activation. Subsequently, the active BTK dissociates from GNA12 to phosphorylate downstream effectors. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964333", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964333" } ] }, { "id": "R-HSA-8964340", "name": "Gq-BTK complex dissociates to Active BTK and Gq", "equation": "", "summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind to the non-receptor Tyrosine-protein kinase BTK. This binding results in a conformational change in BTK. Subsequently, the structurally modified BTK is released from GNAQ and is now catalytically active. Active BTK can trigger the downstream MAPK p38 pathway. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q06187-1" ], "evidence": [ { "id": "R-HSA-8964340", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964340" } ] }, { "id": "R-HSA-937022", "name": "IRAK4 autophosphorylation in the complex with activated TLR:MyD88:TIRAP", "equation": "", "summary": "IRAK4 is activated by autophosphorylation at 3 positions within the kinase activation loop, Thr-342, Thr-345 and Ser-346.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9NWZ3-1", "Q06187-1" ], "evidence": [ { "id": "R-HSA-937022", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-937022" } ] }, { "id": "R-HSA-937059", "name": "Phosphorylation of IRAK2 bound to the activated IRAK4:MyD88 oligomer:TIRAP:activated TLR complex", "equation": "", "summary": "IRAK4 deficient macrophages fail to induce IRAK2 phosphorylation (Kawagoe et al. 2008), suggesting that activated IRAK4 phosphorylates IRAK2 as it does IRAK1.
Phosphorylation sites of IRAK2 remain to be characterized.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9NWZ3-1",
"Q06187-1"
],
"evidence": [
{
"id": "R-HSA-937059",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-937059"
}
]
},
{
"id": "R-HSA-937079",
"name": "MyD88 oligomerization within the complex of activated TLR:TIRAP:MyD88",
"equation": "",
"summary": "Structural analysis of MyD88:IRAK4 and MyD88:IRAK4:IRAK2 suggested that upon MyD88 recruitment to an activated dimerized TLR the MyD88 death domains clustering induces the formation of Mydosome, a large oligomeric signaling platform (Motshwene PG et al 2009, Lin SC et al 2010). Assembly of these Myddosome complexes brings the kinase domains of IRAKs into proximity for phosphorylation and activation. The oligomer complex stoichiometry was reported as 7:4 and 8:4 for MyD88:IRAK4 (Motshwene PG et al 2009), and 6:4:4 in the complex of MyD88:IRAK4:IRAK2(Lin SC et al 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1"
],
"evidence": [
{
"id": "R-HSA-937079",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-937079"
}
]
},
{
"id": "R-HSA-9606151",
"name": "Phosphorylated BLNK (SLP65, in Antigen:p-BCR:p-SYK:p-BLNK:CIN85:GRB2:SOS1) binds BTK, PLCG2, VAV1, NCK1",
"equation": "",
"summary": "Phosphorylated BLNK (also called BASH or SLP-65) at the plasma membrane recruits BTK, PLC gamma, VAV, GRB2, and NCK (Fu and Chan 1997, Fu et al. 1998, Wienands et al. 1998, Su et al. 1999, Baba et al. 2001, Chiu et al. 2002). The SH2 domain of BTK binds phosphorylated BLNK (Hashimoto et al. 1999, Su et al. 1999, Baba et al. 2001). BLNK is constitutively bound to CIN85 and phosphorylated BLNK is bound to a large complex containing CIN85, SOS1, GRB2, phosphorylated SYK, and the B cell receptor.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9606151",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606151"
}
]
},
{
"id": "R-HSA-9606159",
"name": "BTK autophosphorylates",
"equation": "",
"summary": "After phosphorylation on tyrosine-551 by LYN or SYK, BTK autophosphorylates tyrosine-223 (Wahl et al. 1997, Nore et al. 2003, and inferred from mouse homologs). Maximum autophosphorylation occurs 5 minutes after activation of the B cell receptor and returns to low phosphorylation after 30 minutes (Nisitani et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9606159",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606159"
}
]
},
{
"id": "R-HSA-9606162",
"name": "Phosphorylated BTK phosphorylates PLCG2",
"equation": "",
"summary": "Activated BTK (BTK phosphorylated on tyrosine-551 and tyrosine-223) bound to phosphorylated BLNK phosphorylates phospholipase gamma-2 (PKCG2) on tyrosines 753, 759, and 1217 (Rodriguez et al. 2001 and inferred from the rat homolog) thereby activating PLCG2 to hydrolyze phosphatidylinositol 4,5-bisphosphate, yielding the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (Carter et al. 1991, Roifman and Wang 1992, Kim et al. 2004, Sekiya et al. 2004). PLCG2 also binds phosphoinositol 3,4,5-trisphosphate (PIP3) produced by PI3K at the plasma membrane.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9606162",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606162"
}
]
},
{
"id": "R-HSA-9606163",
"name": "p-SYK and LYN phosphorylate BTK",
"equation": "",
"summary": "LYN and activated (phosphorylated) SYK phosphorylate BTK (Baba et al. 2001, Lin et al. 2009, also inferred from chicken homologs and mouse homologs) after BTK is recruited to the plasma membrane by phosphorylated BLNK (Baba et al. 2001) and phosphoinositol 3,4,5-trisphosphate (PIP3) (Salim et al. 1996). Phosphorylation of tyrosine-551 occurs within 30 seconds of B cell receptor activation and returns to low phosphorylation after 30 minutes (Nisitani et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P07948-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9606163",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606163"
}
]
},
{
"id": "R-HSA-9691421",
"name": "BTK binds BTK inhibitors",
"equation": "",
"summary": "Tyrosine-protein kinase BTK (aka Bruton Tyrosine Kinase) is essential for B-cell development and differentiation, and in B-cell receptor signalling. It plays an important role in the function of immune cells of innate and adaptive immunity. BTK inhibitors prevent the proliferation, trafficking, chemotaxis and adhesion of B cells. BTK is also a driving force for chronic lymphocytic leukemia (CLL) and other B cell malignancies.
Ibrutinib is a first-in-class BTK inhibitor that irreversibly binds to Cys-481 in BTK's kinase domain and potently blocks its enzymatic activity (Ponader et al. 2012). It is used to treat CLL and mantle cell lymphoma (MCL).
Acalabrutinib, a second-generation BTK inhibitor, is used for the treatment of CCL (Byrd et al. 2015) and MCL (Cheah et al. 2016). It is in clinical trial in COVID-19 patients as part of the UK's ACCORD initiative. Preliminary data from off-label use in the US suggests that acalabrutinib therapy normalises inflammatory markers such as CRP and IL6 in patients with severe COVID-19. Targeting host hyperinflammation via BTK inhibition may be a rational therapeutic strategy that may improve patient outcomes in this disease (Roschewski et al. 2020).
Other BTK inhibitors which target BTK include spebrutinib, tirabrutinib, naquotinib and zanubrutinib (Tanaka et al. 2020).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9691421",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9691421"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-8863923",
"participant_name": "p-S95-SNAP23 [phagocytic vesicle membrane]",
"crossref": [
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"gene_name": "Flt3",
"activity": [
{
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"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
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{
"uniprot_ac": "A0A0G2K6M9",
"gene_name": "Btk",
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"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
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{
"id": "A0A0G2K6M9",
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]
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{
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"gene_name": "Zap70",
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{
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"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "A0A0R4J8U1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/A0A0R4J8U1"
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}
]
}
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"uniprot_ac": "A0A8I5ZP97",
"gene_name": "Dyrk1b",
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"ec_number": "2.7.12.1",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "A0A8I5ZP97",
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"url": "https://www.uniprot.org/uniprot/A0A8I5ZP97"
}
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}
]
}
]
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"uniprot_ac": "A0A8I5ZVE3",
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"ec_number": "2.7.10.1",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
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{
"id": "A0A8I5ZVE3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/A0A8I5ZVE3"
}
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}
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"gene_name": "Mst1r",
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"ec_number": "2.7.10.1",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "A0A8I6A5T6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/A0A8I6A5T6"
}
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{
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