Oligomerization of Hsp70: Current Perspectives on Regulation and Function

The Hsp70 molecular chaperone in conjunction with Hsp90 and a suite of helper co-chaperones are required for the folding and subsequent refolding of a large proportion of the proteome. These proteins are critical for cell viability and play major roles in diseases of proteostasis which include neuro...

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Bibliographic Details
Published in:Frontiers in molecular biosciences 2019-09, Vol.6, p.81-81
Main Authors: Takakuwa, Jade E, Nitika, Knighton, Laura E, Truman, Andrew W
Format: Article
Language:English
Subjects:
dimerization
Hsp70
Molecular Biosciences
molecular chaperones
oligomerization
proteostasis
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Summary:The Hsp70 molecular chaperone in conjunction with Hsp90 and a suite of helper co-chaperones are required for the folding and subsequent refolding of a large proportion of the proteome. These proteins are critical for cell viability and play major roles in diseases of proteostasis which include neurodegenerative diseases and cancer. As a consequence, a large scientific effort has gone into understanding how chaperones such as Hsp70 function at the and level. Although many chaperones require constitutive self-interaction (dimerization and oligomerization) to function, Hsp70 has been thought to exist as a monomer, especially in eukaryotic cells. Recent studies have demonstrated that both bacterial and mammalian Hsp70 can exist as a dynamic pool of monomers, dimer, and oligomers. In this mini-review, we discuss the mechanisms and roles of Hsp70 oligomerization in Hsp70 function, as well as thoughts on how this integrates into well-established ideas of Hsp70 regulation.
ISSN:2296-889X
2296-889X
DOI:10.3389/fmolb.2019.00081