In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms:
interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001)
intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995)
post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011)
",
"cellular_location": "cytosol",
"input_participant_list": [
"R-ALL-5324631"
],
"output_participant_list": [
"R-HSA-265269",
"R-HSA-3371452"
],
"enzyme_list": [
"P55072-1",
"P07900-1",
"Q15185-1",
"Q9UBN7-1"
],
"evidence": [
{
"id": "R-HSA-5324632",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5324632"
}
]
},
{
"id": "R-HSA-5618331",
"name": "HDAC6 deacetylates microtubules",
"equation": "",
"summary": "HDAC6 is a microtubule-associated deacetylase that targets the K40 acetyl groups of alpha tubulin (Hubbert et al, 2002; Loktev et al, 2008; Zhang et al, 2008). HDAC6 also interacts with BBIP1, a component of the BBSome that is required for BBSome assembly, and additionally (and independently of its role in the BBSome) plays a role in microtubule polymerization and acetylation (Loktev et al, 2008). Depletion of BBIP1 causes a marked reduction in cytoplasmic microtubule acetylation, and this defect is partially overcome by inhibition of HDAC6. These data suggest that BBIP1 may exert its effect on microtubule acetylation by negatively regulating HDAC6, although other mechanisms are also possible (Loktev et al, 2008).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q9UBN7-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-5618331",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618331"
}
]
},
{
"id": "R-HSA-9008389",
"name": "RUNX2 binds HDAC6",
"equation": "",
"summary": "Based on studies in rat osteoblast, RUNX2 forms a complex with the histone deacetylase HDAC6 (Westendorf et al. 2002).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBN7-1"
],
"evidence": [
{
"id": "R-HSA-9008389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9008389"
}
]
},
{
"id": "R-HSA-9008433",
"name": "RUNX2 binds CDKN1A gene promoter",
"equation": "",
"summary": "RUNX2, presumably in complex with at least CBFB, binds to at least two of the three RUNX2-binding sites in the promoter of the CDKN1A (p21) gene. CDK4-mediated phosphorylation of RUNX2 enhances binding of RUNX2 to the CDKN1A promoter (Pierce et al. 2012). The complex of RUNX2 and HDAC6 is also implicated in regulation of the CDKN1A promoter (Westendorf et al. 2002).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBN7-1"
],
"evidence": [
{
"id": "R-HSA-9008433",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9008433"
}
]
},
{
"id": "R-HSA-9008456",
"name": "CDKN1A gene expression is inhibited by RUNX2",
"equation": "",
"summary": "Binding of RUNX2 to the CDKN1A gene promoter inhibits CDKN1A transcription, thus preventing CDKN1A-induced cell cycle arrest. Phosphorylation of RUNX2 by CDK4 in response to high glucose enhances RUNX2-mediated repression of the CDKN1A gene in endothelial cells (Pierce et al. 2012). HDAC6, which forms a complex with RUNX2, may contribute to RUNX2-mediated repression of CDKN1A in developing osteoblasts (Westendorf et al. 2002). In mice, Runx2-mediated repression of Cdkn1a may contribute to the development of acute myeloid leukemia (AML) (Kuo et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBN7-1"
],
"evidence": [
{
"id": "R-HSA-9008456",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9008456"
}
]
},
{
"id": "R-HSA-9615721",
"name": "HSPA8 binds substrate",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds substrate proteins in the cytosol. HSPA8 recognizes a motif based on the charge of the amino acids (Chiang H et al. 1989, Dice JF et al. 1990). This allows the motif to have multiple sequence possibilities and also create a motif through post-translational modifications such as phosphorylation and acetylation. Once bound with HSPA8, the substrates are targeted to the lysosome or endosome.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9615721",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9615721"
}
]
},
{
"id": "R-HSA-9620197",
"name": "HSPA8:Substrate binds LAMP2a",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a) (Cuervo AM and Dice JF. 1996). Four positively charged amino acids in the cytosolic tail of the LAMP2a isoform is known to regulate the binding mechanism (Cuervo AM and Dice JF. 2000). Experiments confirming this binding were performed on rat models.",
"cellular_location": "cytosol, lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9620197",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9620197"
}
]
},
{
"id": "R-HSA-9622831",
"name": "Substrate:LAMP2a binds HSP90",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). HSPA8 is then released from this complex. Subsequently, Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a (Bandyopadhyay U et al. 2008). This facilitates the multimerization of LAMP2a and internalization of substrate into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9622831",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622831"
}
]
},
{
"id": "R-HSA-9622840",
"name": "HSPA8 dissociates from LAMP2A-bound substrate",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Post-binding, HSPA8 is released from the complex to allow multimerization of LAMP2a and internalization of the substrate (Bandyopadhyay U et al. 2008). Experiments confirming this binding were performed on rat models.",
"cellular_location": "cytosol, lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9622840",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622840"
}
]
},
{
"id": "R-HSA-9624158",
"name": "Substrate:LAMP2a:HSP90 polymerizes",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, HSPA8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a. Binding of HSP90 stabilizes LAMP2 to multimerize into a 700 kDa complex (Bandyopadhyay U et al. 2008). This facilitates the internalization of substrate into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9624158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9624158"
}
]
},
{
"id": "R-HSA-9625188",
"name": "HSPA8 transports unfolded substrate to lysosomal lumen for degradation",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from the cytosol to the lysosomal membrane. Subsequently, the substrate unfolds and binds to HSPA8 in the lysosomal lumen. HSPA8 facilitates the transport of the unfolded substrate to the lumen where it is then degraded (Agarraberes FA et al. 1997, Cuervo AM et al. 1997).",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625188",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625188"
}
]
},
{
"id": "R-HSA-9625196",
"name": "Unfolded substrate in LAMP2a multimeric complex binds HSPA8",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds a KFERQ-domain containing substrate in the cytosol and translocates to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, Hspa8 is released and Heat shock protein HSP90 binds to the lysosomal luminal end of LAMP2a. The LAMP2a complex then multimerizes and stabilizes. Now, the substrate unfolds and binds to HSPA8 in the lysosomal lumen (Agarraberes FA et al. 1997, Cuervo AM et al. 1997). Subsequently, the substrate is internalized and degraded in the lumen. Experiments confirming this interaction were performed in rats.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625196",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625196"
}
]
},
{
"id": "R-HSA-9625197",
"name": "GFAP binds LAMP2a multimer",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the HSPA8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, HSPA8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a. This LAMP2a complex then multimerizes into a 700 kDa entity and is stabilized by the binding of Glial fibrillary acidic protein (GFAP) (Bandyopadhyay U et al. 2010). Subsequently, the substrate is unfolded and internalized into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625197",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625197"
}
]
},
{
"id": "R-HSA-9626060",
"name": "HSPA8:Substrate dissociates from LAMP2a multimer",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). The LAMP2a complex then multimerizes and stabilizes. Subsequently, the substrate unfolds and translocates to the lumen. The substrate bound HSPA8 then dissociates from LAMP2a multimer (Agarraberes FA et al. 1997, Cuervo AM et al. 1997). The function of LAMP2a multimer is now complete and starts to disassemble.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9626060",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626060"
}
]
},
{
"id": "R-HSA-9631065",
"name": "Substrate translocates into late endosomal lumen",
"equation": "",
"summary": "In addition to bulk protein degradation, Microautophagy (MI) can also target KFERQ motif protein substrates similar to Chaperone Mediated Autophagy (CMA). However, MI is distinct from CMA in that it occurs during late endosomes/multivesicular bodies formation. Upon binding with Hspa8, substrates are transported from the cytosol to late endosomes. HSPA8 binds with the phospholipids on the late endosomal membrane. Subsequently, the substrate is transported into the lumen via endosomal sorting complexes required for transport (ESCRTI and ESCRTIII systems) (Sahu R et al. 2011). This event is represented as a black box since the precise molecular mechanism of the substrate transport into the endosomal lumen is unclear. Experiments confirming this event were performed in mouse.",
"cellular_location": "cytosol, late endosome membrane, late endosome lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9631065",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9631065"
}
]
},
{
"id": "R-HSA-9631068",
"name": "HSPA8:substrate binds late endosomal phospholipids",
"equation": "",
"summary": "Microautophagy (MI) can target KFERQ motif containing protein substrates to endosomal degradation. Upon binding with HSPA8, substrates are transported from the cytosol to late endosomes. Here, HSPA8 binds with the phospholipids on the late endosomal membrane. This interaction facilitates the vesicle-mediated transport of HSPA8:substrate complex into the late endosomes for degradation (Sahu R et al. 2011). Experiments confirming this interaction were performed in mouse cells.",
"cellular_location": "cytosol, late endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9631068",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9631068"
}
]
},
{
"id": "R-HSA-9646347",
"name": "PolyUb-misfolded proteins bind VCP:HDAC6:HSP90:HSF1",
"equation": "",
"summary": "When the proteasome machinery is deregulated, misfolded proteins are eliminated by forming aggresomes. To this end, poly-ubiquitinated misfolded proteins bind to a complex comprising of Transitional endoplasmic reticulum ATPase (VCP), Histone deacetylase 6 (HDAC6), Heat shock protein HSP 90 (HSP90) and Heat shock factor protein 1 (HSF1). HDAC6 in the complex interacts with the ubiquitin molecules in the misfolded proteins. Following this binding event, this complex starts dissociating (Boyault C et al. 2007).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P55072-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9646347",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646347"
}
]
},
{
"id": "R-HSA-9646348",
"name": "PolyUb-Misfolded Proteins:HDAC6 bind dynein motor",
"equation": "",
"summary": "Histone deacetylase 6 (HDAC6) plays a key role in the removal of misfolded proteins when the proteosome system is dysregulated. HDAC6 associates with poly-ubiquitinated misfolded proteins and also to the dynein motor system. Subsequently, this complex of HDAC6,misfolded proteins and dynein motor form aggresomes (Kawaguchi Y et al. 2003).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q99497-1",
"Q9UBN7-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9646348",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646348"
}
]
},
{
"id": "R-HSA-9646354",
"name": "PolyUb-Misfolded Proteins:HDAC6 dissociate from complex",
"equation": "",
"summary": "Histone deacetylase 6 (HDAC6) appears to be a master regulator of the cell protective response to cytotoxic protein aggregate formation (Boyault et al. 2007).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P55072-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9646354",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646354"
}
]
},
{
"id": "R-HSA-9646383",
"name": "Dynein motors transport misfolded proteins",
"equation": "",
"summary": "Misfolded proteins are transported from the microtubule to the microtubule-organizing center (MTOC) in a dynein-mediated mechanism. Dynein motors carry the cargo along the microtubules from the plus end to the minus end (Garcia Mata R et al. 1999). Confirmatory experiments were performed in grivet cell lines.",
"cellular_location": "cytosol, microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646383",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646383"
}
]
},
{
"id": "R-HSA-9646390",
"name": "Misfolded proteins:HDAC6:Dynein motor binds microtubule",
"equation": "",
"summary": "Histone deacetylase 6 (HDAC6) binds misfolded proteins destined to form aggresomes and subsequently delivers this to dynein motor proteins. HDAC6 can also bind to microtubules thereby anchoring the misfolded proteins and the dynein motor to the microtubule (Hubbert C et al. 2002). Following this, the dynein motors traverse the microtubule to reach the microtubule-organizing center (MTOC).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646390",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646390"
}
]
},
{
"id": "R-HSA-9646679",
"name": "PolyUb-Misfolded proteins bind vimentin to form aggresome",
"equation": "",
"summary": "Dynein motor complex drives the multi-ubiquitinated misfolded proteins along the microtubule towards the microtubule organizing center. Here, intermediate filament proteins such as vimentin (VIM) are redistributed to ensheath misfolded proteins to form the aggresome (Johnston JA et al. 1998). Subsequently, the aggresome is removed with the help of autophagy machinery.",
"cellular_location": "microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646679",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646679"
}
]
},
{
"id": "R-HSA-9646685",
"name": "Aggresome dissociates from dynein and microtubule",
"equation": "",
"summary": "Misfolded proteins are transformed into aggresomes at the microtubule organizing center. Dynein motor proteins facilitate the transport of misfolded proteins along the microtubule. Subsequently, the system disassembles to release the aggresome. The aggresome then recruits chaperone to be degraded by the autophagy machinery (Garcia Mata R et al. 1999).",
"cellular_location": "microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646685",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646685"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-ALL-5324631",
"participant_name": "Ub-protein aggregates [cytosol]",
"crossref": [
{
"id": "23367",
"database": "ChEBI",
"url": ""
},
{
"id": "23367",
"database": "ChEBI",
"url": ""
},
{
"id": "23367",
"database": "ChEBI",
"url": ""
},
{
"id": "23367",
"database": "ChEBI",
"url": ""
},
{
"id": "23367",
"database": "ChEBI",
"url": ""
},
{
"id": "23367",
"database": "ChEBI",
"url": ""
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