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Septins: Regulators of Protein Stability

Septins are small GTPases that play a role in several important cellular processes. In this review, we focus on the roles of septins in protein stabilization. Septins may regulate protein stability by: (1) interacting with proteins involved in degradation pathways, (2) regulating the interaction bet...

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Detalles Bibliográficos
Autores principales: Vagin, Olga, Beenhouwer, David O.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5168428/
https://www.ncbi.nlm.nih.gov/pubmed/28066764
http://dx.doi.org/10.3389/fcell.2016.00143
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author Vagin, Olga
Beenhouwer, David O.
author_facet Vagin, Olga
Beenhouwer, David O.
author_sort Vagin, Olga
collection PubMed
description Septins are small GTPases that play a role in several important cellular processes. In this review, we focus on the roles of septins in protein stabilization. Septins may regulate protein stability by: (1) interacting with proteins involved in degradation pathways, (2) regulating the interaction between transmembrane proteins and cytoskeletal proteins, (3) affecting the mobility of transmembrane proteins in lipid bilayers, and (4) modulating the interaction of proteins with their adaptor or signaling proteins. In this context, we discuss the role of septins in protecting four different proteins from degradation. First we consider botulinum neurotoxin serotype A (BoNT/A) and the contribution of septins to its extraordinarily long intracellular persistence. Next, we discuss the role of septins in stabilizing the receptor tyrosine kinases EGFR and ErbB2. Finally, we consider the contribution of septins in protecting hypoxia-inducible factor 1α (HIF-1α) from degradation.
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spelling pubmed-51684282017-01-06 Septins: Regulators of Protein Stability Vagin, Olga Beenhouwer, David O. Front Cell Dev Biol Cell and Developmental Biology Septins are small GTPases that play a role in several important cellular processes. In this review, we focus on the roles of septins in protein stabilization. Septins may regulate protein stability by: (1) interacting with proteins involved in degradation pathways, (2) regulating the interaction between transmembrane proteins and cytoskeletal proteins, (3) affecting the mobility of transmembrane proteins in lipid bilayers, and (4) modulating the interaction of proteins with their adaptor or signaling proteins. In this context, we discuss the role of septins in protecting four different proteins from degradation. First we consider botulinum neurotoxin serotype A (BoNT/A) and the contribution of septins to its extraordinarily long intracellular persistence. Next, we discuss the role of septins in stabilizing the receptor tyrosine kinases EGFR and ErbB2. Finally, we consider the contribution of septins in protecting hypoxia-inducible factor 1α (HIF-1α) from degradation. Frontiers Media S.A. 2016-12-20 /pmc/articles/PMC5168428/ /pubmed/28066764 http://dx.doi.org/10.3389/fcell.2016.00143 Text en Copyright © 2016 Vagin and Beenhouwer. 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) or licensor 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 Cell and Developmental Biology
Vagin, Olga
Beenhouwer, David O.
Septins: Regulators of Protein Stability
title Septins: Regulators of Protein Stability
title_full Septins: Regulators of Protein Stability
title_fullStr Septins: Regulators of Protein Stability
title_full_unstemmed Septins: Regulators of Protein Stability
title_short Septins: Regulators of Protein Stability
title_sort septins: regulators of protein stability
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5168428/
https://www.ncbi.nlm.nih.gov/pubmed/28066764
http://dx.doi.org/10.3389/fcell.2016.00143
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