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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6742908/ https://www.ncbi.nlm.nih.gov/pubmed/31555664 http://dx.doi.org/10.3389/fmolb.2019.00081 |
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author | Takakuwa, Jade E. Nitika, Knighton, Laura E. Truman, Andrew W. |
author_facet | Takakuwa, Jade E. Nitika, Knighton, Laura E. Truman, Andrew W. |
author_sort | Takakuwa, Jade E. |
collection | PubMed |
description | 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 in vitro and in vivo 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. |
format | Online Article Text |
id | pubmed-6742908 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-67429082019-09-25 Oligomerization of Hsp70: Current Perspectives on Regulation and Function Takakuwa, Jade E. Nitika, Knighton, Laura E. Truman, Andrew W. Front Mol Biosci Molecular Biosciences 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 in vitro and in vivo 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. Frontiers Media S.A. 2019-09-04 /pmc/articles/PMC6742908/ /pubmed/31555664 http://dx.doi.org/10.3389/fmolb.2019.00081 Text en Copyright © 2019 Takakuwa, Nitika, Knighton and Truman. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Takakuwa, Jade E. Nitika, Knighton, Laura E. Truman, Andrew W. Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title_full | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title_fullStr | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title_full_unstemmed | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title_short | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
title_sort | oligomerization of hsp70: current perspectives on regulation and function |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6742908/ https://www.ncbi.nlm.nih.gov/pubmed/31555664 http://dx.doi.org/10.3389/fmolb.2019.00081 |
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