Publication:
Regulation of protein turnover by heat shock proteins

Simple item page
dc.contributor.authorYILMAZ, BETÜL
dc.contributor.authorsBozaykut, Perinur; Ozer, Nesrin Kartal; Karademir, Betul
dc.date.accessioned2022-03-10T15:25:14Z
dc.date.available2022-03-10T15:25:14Z
dc.date.issued2014
dc.description.abstractProtein turnover reflects the balance between synthesis and degradation of proteins, and it is a crucial process for the maintenance of the cellular protein pool. The folding of proteins, refolding of misfolded proteins, and also degradation of misfolded and damaged proteins are involved in the protein quality control (PQC) system. Correct protein folding and degradation are controlled by many different factors, one of the most important of which is the heat shock protein family. Heat shock proteins (HSPs) are in the class of molecular chaperones, which may prevent the inappropriate interaction of proteins and induce correct folding. On the other hand, these proteins play significant roles in the degradation pathways, including endoplasmic reticulum-associated degradation (ERAD), the ubiquitin-proteasome system, and autophagy. This review focuses on the emerging role of HSPs in the regulation of protein turnover; the effects of HSPs on the degradation machineries ERAD, autophagy, and proteasome; as well as the role of posttranslational modifications in the PQC system. (C) 2014 Elsevier Inc. All rights reserved.
dc.identifier.doi10.1016/j.freeradbiomed.2014.08.012
dc.identifier.eissn1873-4596
dc.identifier.issn0891-5849
dc.identifier.pubmed25236750
dc.identifier.urihttps://hdl.handle.net/11424/220165
dc.identifier.wosWOS:000346392500019
dc.language.isoeng
dc.publisherELSEVIER SCIENCE INC
dc.relation.ispartofFREE RADICAL BIOLOGY AND MEDICINE
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectHeat shock proteins
dc.subjectProtein turnover
dc.subjectProteasome
dc.subjectAutophagy
dc.subjectProtein quality system
dc.subjectPosttranslational modifications
dc.subjectFree radicals
dc.subjectUBIQUITIN-PROTEASOME SYSTEM
dc.subjectCHAPERONE-MEDIATED AUTOPHAGY
dc.subjectHSP90 INHIBITOR GELDANAMYCIN
dc.subjectBCL-X-L
dc.subjectTETHERED MOLECULAR CHAPERONES
dc.subjectSTARVATION-INDUCED AUTOPHAGY
dc.subjectALPHA-B-CRYSTALLIN
dc.subjectI-KAPPA-B
dc.subjectQUALITY-CONTROL
dc.subjectENDOPLASMIC-RETICULUM
dc.titleRegulation of protein turnover by heat shock proteins
dc.typereview
dspace.entity.typePublication
local.avesis.idbd535d2f-03ba-461a-96ee-74e59b451880
local.import.packageSS5
local.indexed.atWOS
local.indexed.atSCOPUS
local.indexed.atPUBMED
local.journal.numberofpages15
oaire.citation.endPage209
oaire.citation.startPage195
oaire.citation.titleFREE RADICAL BIOLOGY AND MEDICINE
oaire.citation.volume77
relation.isAuthorOfPublication81633a07-e5fb-4760-b3ef-bf0878d87827
relation.isAuthorOfPublication.latestForDiscovery81633a07-e5fb-4760-b3ef-bf0878d87827

Files

Collections

Research Outputs