The functional importance of VCP to maintaining cellular protein homeostasis

The AAA-ATPase (ATPases associated with diverse cellular activities) valosin-containing protein (VCP), is essential for many cellular pathways including but not limited to endoplasmic reticulum-associated degradation (ERAD), DNA damage responses, and cell cycle regulation. VCP primarily identifies u...

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Detalles Bibliográficos
Autores principales: Ahlstedt, Brittany A., Ganji, Rakesh, Raman, Malavika
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2022
Materias:
Review Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9704522/
https://www.ncbi.nlm.nih.gov/pubmed/36196920
http://dx.doi.org/10.1042/BST20220648
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author Ahlstedt, Brittany A.
Ganji, Rakesh
Raman, Malavika
author_facet Ahlstedt, Brittany A.
Ganji, Rakesh
Raman, Malavika
author_sort Ahlstedt, Brittany A.
collection PubMed
description The AAA-ATPase (ATPases associated with diverse cellular activities) valosin-containing protein (VCP), is essential for many cellular pathways including but not limited to endoplasmic reticulum-associated degradation (ERAD), DNA damage responses, and cell cycle regulation. VCP primarily identifies ubiquitylated proteins in these pathways and mediates their unfolding and degradation by the 26S proteasome. This review summarizes recent research on VCP that has uncovered surprising new ways that this ATPase is regulated, new aspects of recognition of substrates and novel pathways and substrates that utilize its activity.
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spelling pubmed-97045222022-12-06 The functional importance of VCP to maintaining cellular protein homeostasis Ahlstedt, Brittany A. Ganji, Rakesh Raman, Malavika Biochem Soc Trans Review Articles The AAA-ATPase (ATPases associated with diverse cellular activities) valosin-containing protein (VCP), is essential for many cellular pathways including but not limited to endoplasmic reticulum-associated degradation (ERAD), DNA damage responses, and cell cycle regulation. VCP primarily identifies ubiquitylated proteins in these pathways and mediates their unfolding and degradation by the 26S proteasome. This review summarizes recent research on VCP that has uncovered surprising new ways that this ATPase is regulated, new aspects of recognition of substrates and novel pathways and substrates that utilize its activity. Portland Press Ltd. 2022-10-31 2022-10-05 /pmc/articles/PMC9704522/ /pubmed/36196920 http://dx.doi.org/10.1042/BST20220648 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review Articles
Ahlstedt, Brittany A.
Ganji, Rakesh
Raman, Malavika
The functional importance of VCP to maintaining cellular protein homeostasis
title The functional importance of VCP to maintaining cellular protein homeostasis
title_full The functional importance of VCP to maintaining cellular protein homeostasis
title_fullStr The functional importance of VCP to maintaining cellular protein homeostasis
title_full_unstemmed The functional importance of VCP to maintaining cellular protein homeostasis
title_short The functional importance of VCP to maintaining cellular protein homeostasis
title_sort functional importance of vcp to maintaining cellular protein homeostasis
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9704522/
https://www.ncbi.nlm.nih.gov/pubmed/36196920
http://dx.doi.org/10.1042/BST20220648
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