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Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins

In plants, AAA-adenosine triphosphatase (ATPase) Cell Division Control Protein 48 (CDC48) uses the force generated through ATP hydrolysis to pull, extract, and unfold ubiquitylated or sumoylated proteins from the membrane, chromatin, or protein complexes. The resulting changes in protein or RNA cont...

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Autores principales: Zhang, Junrui, Vancea, Alexandra I., Shahul Hameed, Umar F., Arold, Stefan T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8181520/
https://www.ncbi.nlm.nih.gov/pubmed/34141135
http://dx.doi.org/10.1016/j.csbj.2021.05.025
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author Zhang, Junrui
Vancea, Alexandra I.
Shahul Hameed, Umar F.
Arold, Stefan T.
author_facet Zhang, Junrui
Vancea, Alexandra I.
Shahul Hameed, Umar F.
Arold, Stefan T.
author_sort Zhang, Junrui
collection PubMed
description In plants, AAA-adenosine triphosphatase (ATPase) Cell Division Control Protein 48 (CDC48) uses the force generated through ATP hydrolysis to pull, extract, and unfold ubiquitylated or sumoylated proteins from the membrane, chromatin, or protein complexes. The resulting changes in protein or RNA content are an important means for plants to control protein homeostasis and thereby adapt to shifting environmental conditions. The activity and targeting of CDC48 are controlled by adaptor proteins, of which the plant ubiquitin regulatory X (UBX) domain-containing (PUX) proteins constitute the largest family. Emerging knowledge on the structure and function of PUX proteins highlights that these proteins are versatile factors for plant homeostasis and adaptation that might inspire biotechnological applications.
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spelling pubmed-81815202021-06-16 Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins Zhang, Junrui Vancea, Alexandra I. Shahul Hameed, Umar F. Arold, Stefan T. Comput Struct Biotechnol J Review Article In plants, AAA-adenosine triphosphatase (ATPase) Cell Division Control Protein 48 (CDC48) uses the force generated through ATP hydrolysis to pull, extract, and unfold ubiquitylated or sumoylated proteins from the membrane, chromatin, or protein complexes. The resulting changes in protein or RNA content are an important means for plants to control protein homeostasis and thereby adapt to shifting environmental conditions. The activity and targeting of CDC48 are controlled by adaptor proteins, of which the plant ubiquitin regulatory X (UBX) domain-containing (PUX) proteins constitute the largest family. Emerging knowledge on the structure and function of PUX proteins highlights that these proteins are versatile factors for plant homeostasis and adaptation that might inspire biotechnological applications. Research Network of Computational and Structural Biotechnology 2021-05-14 /pmc/articles/PMC8181520/ /pubmed/34141135 http://dx.doi.org/10.1016/j.csbj.2021.05.025 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review Article
Zhang, Junrui
Vancea, Alexandra I.
Shahul Hameed, Umar F.
Arold, Stefan T.
Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title_full Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title_fullStr Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title_full_unstemmed Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title_short Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
title_sort versatile control of the cdc48 segregase by the plant ubx-containing (pux) proteins
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8181520/
https://www.ncbi.nlm.nih.gov/pubmed/34141135
http://dx.doi.org/10.1016/j.csbj.2021.05.025
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