Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation

Heat shock protein 70 (Hsp70) is a molecular chaperone required for protein folding, cell viability, and cancer cell proliferation. Recent studies suggest that Hsp70 phosphorylation regulates important cellular processes, such as cell cycle progression, apoptosis, protein degradation, and resistance...

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Veröffentlicht in:	Trends in biochemical sciences (Amsterdam. Regular ed.) 2017-12, Vol.42 (12), p.932-935
Hauptverfasser:	Nitika, Truman, Andrew W.
Format:	Artikel
Sprache:	eng
Schlagworte:	antineoplastic agents Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology apoptosis Apoptosis - drug effects cancer cell cycle cell proliferation Cell Proliferation - drug effects Cell Survival - drug effects cell viability chaperones heat-shock protein 70 Hsp70 HSP70 Heat-Shock Proteins - antagonists & inhibitors HSP70 Heat-Shock Proteins - metabolism Humans kinases Molecular Chaperones - antagonists & inhibitors Molecular Chaperones - metabolism neoplasms phosphorylation Phosphorylation - drug effects protein degradation protein folding
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Beschreibung
Zusammenfassung:	Heat shock protein 70 (Hsp70) is a molecular chaperone required for protein folding, cell viability, and cancer cell proliferation. Recent studies suggest that Hsp70 phosphorylation regulates important cellular processes, such as cell cycle progression, apoptosis, protein degradation, and resistance to anticancer therapeutics.
ISSN:	0968-0004 1362-4326
DOI:	10.1016/j.tibs.2017.10.002