The importance of being chaperoned: HSP90 and necroptosis

Annette V Jacobsen; John Silke

doi:10.1016/j.chembiol.2016.02.003

The importance of being chaperoned: HSP90 and necroptosis

Cell Chem Biol. 2016 Feb 18;23(2):205-207. doi: 10.1016/j.chembiol.2016.02.003.

Authors

Annette V Jacobsen¹, John Silke²

Affiliations

¹ The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, Australia.
² The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, Australia. Electronic address: silke@wehi.edu.au.

PMID: 26971869
DOI: 10.1016/j.chembiol.2016.02.003

Abstract

Necroptosis is a form of regulated cell death implicated in a range of inflammatory diseases. In this issue of Cell Chemical Biology, Li et al. (2016) describe a novel inhibitor of necroptosis that targets the chaperone protein HSP90.

Publication types

Comment

MeSH terms

Apoptosis
Cell Death
Cell Line, Tumor
Cell Survival
HSP70 Heat-Shock Proteins / metabolism
HSP72 Heat-Shock Proteins / metabolism
HSP90 Heat-Shock Proteins / metabolism*
Humans
Molecular Chaperones / metabolism
Necrosis / metabolism*
Protein Kinases / metabolism
Receptor-Interacting Protein Serine-Threonine Kinases / metabolism
Signal Transduction

Substances

HSP70 Heat-Shock Proteins
HSP72 Heat-Shock Proteins
HSP90 Heat-Shock Proteins
Molecular Chaperones
Protein Kinases
Receptor-Interacting Protein Serine-Threonine Kinases