RIPK3 binds HSP90:CDC37

Stable Identifier
R-HSA-9688459
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Synonyms
RIPK3+ HSP90 homodimer + CDC37 homodimer => RIPK3:HSP90:CDC37
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Receptor-interacting serine/threonine protein kinase 3 (RIPK3 or RIP3) activation following the induction of necroptosis in human HT-29 colorectal adenocarcinoma cells requires the activity of a heat-shock protein 90 (HSP90) and cell division cycle 37 (CDC37) cochaperone complex (Li D et al. 2015). This complex physically associates with RIPK3. Chemical inhibitors of HSP90 efficiently block necroptosis by preventing RIP3 activation in HT-29. Cells with knocked down CDC37 were unable to respond to necroptosis stimuli (Li D et al. 2015). Further, geldanamycin, an inhibitor of HSP90, and siRNA/shRNA of HSP90α, protected cultured neurons from oxygen-glucose deprivation induced necroptosis by decreasing RIP3 expression (Wang Z et al. 2018). Geldanamycin was reported to nhibit programmed necrosis by suppressing RIPK3 protein expression (Cho YS et al. 2009).Moreover, the HSP90:CDC37 complex was found to interact and regulate the stability of mixed lineage kinase domain-like (MLKL), the downstream effector of the necroptotic signalling pathway (Bigenzahn JW et al. 2016; Jacobsen AV et al. 2016; Zhao XM et al. 2016).

Literature References
PubMed ID Title Journal Year
25852146 A cytosolic heat shock protein 90 and cochaperone CDC37 complex is required for RIP3 activation during necroptosis

Li, D, Xu, T, Cao, Y, Wang, H, Li, L, Chen, S, Wang, X, Shen, Z

Proc. Natl. Acad. Sci. U.S.A. 2015
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