The presence of MTP:PDI (microsomal triacylglycerol transfer protein:protein disulfide isomerase) is required for lipid addition both in vitro and in vivo, but its molecular role at this stage of chylomicron formation is unclear and may be indirect (Gordon et al. 1995; Hussain et al. 2003).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-174741",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-174741"
}
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},
{
"id": "R-HSA-174786",
"name": "ApoB-48 + 40 triacylglycerol + 60 phospholipid => ApoB-48:TG:PL complex",
"equation": "",
"summary": "Phospholipid (PL) and triacylglycerol (TG) associate with the apo B-48 polypeptide as it is translated. This process is mediated by MTP (microsomal triacylglycerol transfer protein) in the form of a MTP:PDI (protein disulfide isomerase) heterodimer. MTP in vitro binds small amounts of PL and TG (annotated here as as one molecule of each) and efficiently transfers the bound lipid between membranes (Atzel and Wetterau 1994). In vivo, MTP:PDI directly interacts with apoB-48 polypeptide (Wu et al. 1996), and is thought to transfer lipid from the endoplasmic reticulum membrane to nascent apoB-48. While some of the molecular details of MTP function remain unclear, this function is clearly essential in vivo, as patients who lack MTP cannot produce chylomicrons (e.g., Wetterau et al. 1992; Narcisi et al. 1995).",
"cellular_location": "endoplasmic reticulum lumen, endoplasmic reticulum membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-174786",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-174786"
}
]
},
{
"id": "R-HSA-2002460",
"name": "P4HB binds Collagen chains",
"equation": "",
"summary": "As the collagen peptide chain is translocated across the membrane of the endoplasmic reticulum, intrachain disulfide bonds are formed within the N- and C-propeptides. This allows the triple helical domain to form a nucleation point at its C-terminal end and ensures correct alignment of the chains (Engel & Prockop 1991). Protein disulfide isomerase (P4HB) catalyzes the formation of both intra- (Bulleid & Freedman 1988) and inter-chain disulfide bonds (Koivu & Myllyl\u00e4 1987). In addition, PDI acts as a molecular chaperone, interacting with monomeric collagen propeptide chains to prevent premature assembly or aggregation (Wilson et al. 1998).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-2002460",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2002460"
}
]
},
{
"id": "R-HSA-264997",
"name": "P4HB mediates disulfide bond formation in Proinsulin",
"equation": "",
"summary": "In vitro, P4HB (PDIA1) in its oxidized form (HC53,56-P4HB) mediates the correct folding of proinsulin with disulfide bond formation and is itself reduced to P4HB (Hudson et al. 2015; Winter et al. 2011). Studies of insulin processing in knockout mutant mice are consistent with this role for P4HB, while also suggesting that other disulfide isomerases, not annotated here, could play a role in this process in vivo (Jang et al. 2019).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [
"R-HSA-3341287"
],
"output_participant_list": [
"R-HSA-265075"
],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-264997",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-264997"
}
]
},
{
"id": "R-HSA-3341296",
"name": "GPX7,8 catalyze peroxidation of P4HB (PDI)",
"equation": "",
"summary": "Glutathione peroxidase 7 (GPX7) and GPX8 are atypical glutathione peroxidases that catalyze the peroxidation of protein disulfide isomerases, such as PDI (P4HB) (Nguyen et al. 2011 and inferred from mouse in Bosello-Travain et al. 2013). GPX7 and GPX8 are each able to form heterodimers with the sulfhydryl oxidase ERO1alpha (ERO1L) in the endoplasmic reticulum lumen. It is hypothesized that GPX7 and GPX8 use hydrogen peroxide produced by ERO1L.",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [
"R-ALL-3341383",
"R-HSA-174692"
],
"output_participant_list": [],
"enzyme_list": [
"Q8TED1-1",
"P07237-1",
"Q96HE7-1",
"Q96SL4-1"
],
"evidence": [
{
"id": "R-HSA-3341296",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3341296"
}
]
},
{
"id": "R-HSA-5358336",
"name": "P4HB forms mixed disulphides with Hh precursors",
"equation": "",
"summary": "Hh ligands undergo a autoproteolytic cleavage mediated by a conserved residue in the C-terminal region to yield an N-terminal fragment destined for further modification and secretion, and a C-terminal fragment that is subsequently degraded by ERAD (reviewed in Gallet, 2011). Recent work has shown that autoproteolytic cleavage of Hh ligands depends on prior formation of an intramolecular disulphide bond between the catalytic cysteine residue and another conserved cysteine residue in the C-terminal region of the precursor (Chen et al, 2011). Mutation of either of these cysteine residues abolishes cleavage, suggesting that the intramolecular disulphide bond is required to establish a catalytically active conformation of the precursor (Chen et al, 2011).
Prior to the autoproteolytic cleavage reaction, the protein disulphide isomerase P4HB is required to reduce the intramolecular disulphide, freeing the catalytic cysteine side chain for nucleophilic attack. Mutational analysis and co-immunoprecipitation studies support a model where the N-terminal CXXC motif of P4HB forms a mixed disulphide with the non-catalytic cysteine residue of the Hh precursor (Chen et al, 2011.",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43323-1",
"P07237-1",
"Q15465-1",
"Q14623-1"
],
"evidence": [
{
"id": "R-HSA-5358336",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5358336"
}
]
},
{
"id": "R-HSA-5358340",
"name": "Autoproteolytic cleavage of Hh precursors",
"equation": "",
"summary": "Autoproteolytic processing of the Hh precursor is essential for the production of active secreted Hh ligand and mutants that disrupt this processing have been identified in the congenital nervous system disorder holoprosencephaly (Traiffort et al, 2004; Maity et al, 2005; Roessler et al, 2009; reviewed in Jiang et al, 2008). Cleavage of Hh occurs through two nucleophilic substitutions. The first step is mediated by the catalytic cysteine residue, which is found in a conserved G-C-F motif. The cysteine side chain attacks the carbonyl carbon of the main peptide chain between the glycine and cysteine residues, replacing the amino group in the peptide backbone with a thioester linkage (Lee et al, 1994; Porter et al, 1995; Porter et al, 1996a, b; Chen et al, 2011). The second step involves nucleophilic attack of the same carbonyl group by cholesterol. This step displaces the C-terminal fragment (Hh-C) of the Hh precursor and results in the formation of the N-terminal fragment (Hh-Np) modified at its C-terminus by an ester linkage with cholesterol (Porter et al, 1996a, b; Chen et al, 2011). Cholesterol modification appears to contribute to further processing and trafficking of the Hh ligand, as engineered forms of vertebrate and fly Hh that lack cholesterol are not efficiently palmitoylated (Pepinsky et al, 1998). Cholesterol also restricts the diffusion of the secreted ligand by interacting with the lipid bilayer of the secreting cell. Consistent with this, aberrant activation of Hh target genes is seen in the absence of cholesterol modification (Peters et al, 2004; Guerrero et al, 2007; Li et al, 2006; Huang et al, 2007).
",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [
"R-ALL-174672"
],
"output_participant_list": [],
"enzyme_list": [
"O43323-1",
"P07237-1",
"Q15465-1",
"Q14623-1"
],
"evidence": [
{
"id": "R-HSA-5358340",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5358340"
}
]
},
{
"id": "R-HSA-8866329",
"name": "MTTP lipidates APOB-100, forming a pre-VLDL",
"equation": "",
"summary": "The assembly of very low-density lipoprotein (VLDL) occurs in two steps (Olofsson et al. 2000). In the first step, apolipoprotein B-100 (APOB(28-4563), APOB-100) is co- and post-translationally lipidated by MTP (microsomal triacylglycerol transfer protein) in the form of a MTP:PDI (protein disulfide isomerase) heterodimer (Gordon et al. 1995), forming a pre-VLDL. This occurs in the rough endoplasmic reticulum (RER) lumen. The pre-VLDL is loosely associated with the RER membrane. MTP in vitro binds small amounts of PL and TAG (annotated here as one molecule of each) and efficiently transfers the bound lipid between membranes (Atzel & Wetterau 1994). In vivo, MTP:PDI directly interacts with APOB-100 polypeptide (Wu et al. 1996), and is thought to transfer lipid from the endoplasmic reticulum membrane to nascent APOB-100. In humans, APOB-100 is expressed in the liver and forms VLDL whereas APOB-48 is expressed in the intestine and forms chylomicrons.",
"cellular_location": "endoplasmic reticulum lumen, endoplasmic reticulum membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-8866329",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8866329"
}
]
},
{
"id": "R-HSA-8948234",
"name": "P4HB:4-Hyp collagen propeptides dissociates",
"equation": "",
"summary": "Following the formation of 4-hydroxyproline residues by prolyl 4-hydroxylase, the modified collagen chain dissociates.",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-8948234",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8948234"
}
]
},
{
"id": "R-HSA-8950113",
"name": "IL12A binds IL12B",
"equation": "",
"summary": "The Interleukin-12 heterodimer (IL-12) is formed by Interleukin-12 subunit alpha (IL12A, IL-12p35) and Interleukin-12 subunit beta (IL12B, IL-12p40) (Podlaski et al. 1992, Kobayashi et al. 1989, Stern et al.1990). Heterodimerization occurs due to charged residue interactions (Yoon et al. 2000) and is stabilized by disulfide bounding.
IL12 heterodimerization is believed to occur in the endoplasmic reticulum (ER) because inhibition of the enzyme Prolyl 4-hydroxylase subunit beta (P4HB), referred to in this article as Protein disulfide isomerase (PDI), by bacitracin causes IL-12 retention in the ER (Alloza & Vandenbroek 2005).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-8950113",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950113"
}
]
},
{
"id": "R-HSA-8950183",
"name": "IL12B binds IL23A",
"equation": "",
"summary": "Interleukin 23 subunit alpha (IL23A, IL23-p19) and Interleukin 12 subunit beta (IL12B, IL-12p40) bind to form the Interleukin-23 (IL23) heterodimeric complex (IL23A:IL12B). When 293T cells were transfected with IL23A only a small amount of protein could be immunoprecipitated from the supernatant, while protein was readily detected in cellular lysates, indicating inefficient secretion. Co expression of IL23A with IL12B enhanced secretion of IL23 (Oppmann et al. 2000). Moreover there is a disulfide bridge within IL12A which is necessary fro IL12B-induced secretion. Protein disulfide isomerases enable the formation of these bridges (Reitberger et al. 2017).;",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-8950183",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950183"
}
]
},
{
"id": "R-HSA-8950456",
"name": "IL12B dimerizes",
"equation": "",
"summary": "Murine cells have been shown to produce Interleukin-12 homodimer (IL-12p80) (Gillessen et al. 1995). In a cell-free system porcine Interleukin 12 homodimer (IL-12p80) is formed from two subunits of Interleukin 12 subunit beta (IL12B, IL-12p40), stabilized by a disulfide link. The cysteine in position 197 of IL12B is required for homodimer formation. Prolyl 4-hydroxylase subunit beta (P4HB), in this article referred to as protein disulfide isomerase (PDI), can act as a chaperone to induce homodimer formation (Martens et al. 2000). Human cells do not produce IL-12p80 under normal conditions (Ling et al. 1995), when however expressed acts as an antagonist of Interleukin-12 signaling, competing with the Interleukin 12 heterodimer (IL12) for its receptor (Ling et al. 1995).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-8950456",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950456"
}
]
},
{
"id": "R-HSA-8952289",
"name": "FAM20C phosphorylates FAM20C substrates",
"equation": "",
"summary": "Extracellular serine/threonine protein kinase FAM20C is an extracellular kinase that can phosphorylate a broad range of secreted protein. FAM20C is bound and allosterically activated by the pseudokinase FAM20A (Tagliabracchi et al. 2012, 2015, Cui et al. 2015).
Loss of function mutations in Fam20C cause Raine Syndrome, an osteosclerotic bone dysplasia (Faundes et al. 2014).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [
"R-ALL-8931885"
],
"output_participant_list": [
"R-ALL-8931884"
],
"enzyme_list": [
"Q6P988-1",
"P07237-1",
"O14672-1",
"Q8NBP7-1",
"Q8IXL6-1",
"P00450-1",
"P04070-1",
"Q9BTY2-1",
"Q96AD5-1",
"Q14703-1",
"Q9UM21-1",
"Q15084-1",
"O95084-1",
"O00391-1"
],
"evidence": [
{
"id": "R-HSA-8952289",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8952289"
}
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{
"id": "R-HSA-9737780",
"name": "MTTP binds lomitapide",
"equation": "",
"summary": "The microsomal triglyceride transfer protein (MTTP) is required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. The discovery of a mutation in the MTTP gene causing abetalipoproteinemia (Ricci et al. 1995) was essential for the development of drugs to inhibit MTTP (Jamil et al. 1996, Chang et al. 2002).
The pharmacological inhibition of MTTP by lomitapide is associated with a decrease in LDL cholesterol (LDL-C) and triglycerides (Cuchel et al. 2007). Lomitapide significantly reduces LDL-C in homozygous familial hypercholesterolemia (hFH) (Samaha et al. 2008, Cuchel et al. 2013) when administered concurrently with other lipid-lowering therapies (Stefanutti 2020). Lomitapide can lead to elevated aminotransferase levels and fat accumulation in the liver (Cuchel et al. 2007).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07237-1"
],
"evidence": [
{
"id": "R-HSA-9737780",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9737780"
}
]
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{
"id": "R-HSA-9817575",
"name": "ERO1B oxidizes P4HB",
"equation": "",
"summary": "ERO1B catalyzes the reduction of the disulfide bond in HC53,56-P4HB to form P4HB plus H2O2 (Gross et al. 2006; Mezghrani et al. 2001; Wang et al. 2011). Studies of knockout mutant mice are consistent with this role for ERO1B, while also suggesting that other oxidoreductases, not annotated here, could play a role in this process in vivo (Zito et al. 2010a b). See also the review of oxidative protein folding by Hudson et al. (2015).",
"cellular_location": "endoplasmic reticulum lumen",
"input_participant_list": [],
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"P07237-1",
"Q86YB8-1"
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"evidence": [
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"id": "R-HSA-9817575",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9817575"
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}
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