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PMID: 15770419 Published · ppublish English Journal Article Review

Hsp70 chaperones: cellular functions and molecular mechanism.

Cellular and molecular life sciences : CMLS ·Vol. 62 ·No. 6 ·2005-03-00 ·Pages 670-84

Mayer MP, Bukau B

Abstract

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.

MeSH Terms
Adenosine Triphosphatases/chemistry,metabolism Animals Bacterial Proteins/chemistry,metabolism Binding Sites Carrier Proteins/metabolism Cell Physiological Phenomena DNA-Binding Proteins HSP70 Heat-Shock Proteins/chemistry,metabolism Models, Molecular Molecular Chaperones/metabolism Protein Folding Protein Structure, Tertiary Transcription Factors Ubiquitin-Protein Ligases/metabolism
Chemicals
BCL2-associated athanogene 1 protein Bacterial Proteins Carrier Proteins DNA-Binding Proteins HSP70 Heat-Shock Proteins Hip chaperone Molecular Chaperones Transcription Factors Ubiquitin-Protein Ligases Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mayer M P
Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany. [email protected]
Bukau B
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Article Info
Journal
Cellular and molecular life sciences : CMLS
Abbr.
Cell Mol Life Sci
ISSN
1420-682X
DOI
10.1007/s00018-004-4464-6
Email
[email protected]
Published
2005-03-00
Pages
670-84
Language
English
Region
Switzerland
NLM ID
9705402
PMCID
PMC2773841
Subset
IM
External Links
PubMed source DOI: 10.1007/s00018-004-4464-6 PMC Full Text View journal details
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