Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42

Summary: Cdc42 GTPase rules cell polarity and growth in fission yeast. It is negatively and positively regulated by GTPase-activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), respectively. Active Cdc42-GTP localizes to the poles, where it associates with numerous proteins cons...

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Autores principales:	Clàudia Salat-Canela, Mercè Carmona, Rebeca Martín-García, Pilar Pérez, José Ayté, Elena Hidalgo
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Sty1 Cdc42 cell polarity stress response cell size GAP Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6387bfcfd2c149ada5f5a78fed45275b
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spelling	oai:doaj.org-article:6387bfcfd2c149ada5f5a78fed45275b2021-11-04T04:29:47ZStress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc422211-124710.1016/j.celrep.2021.109951https://doaj.org/article/6387bfcfd2c149ada5f5a78fed45275b2021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2211124721014285https://doaj.org/toc/2211-1247Summary: Cdc42 GTPase rules cell polarity and growth in fission yeast. It is negatively and positively regulated by GTPase-activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), respectively. Active Cdc42-GTP localizes to the poles, where it associates with numerous proteins constituting the polarity module. However, little is known about its downregulation. We describe here that oxidative stress causes Sty1-kinase-dependent Cdc42 inactivation at cell poles. Both the amount of active Cdc42 at tips and cell length inversely correlate with Sty1 activity, explaining the elongated morphology of Δsty1 cells. We have created stress-blinded cell poles either by eliminating two Cdc42 GAPs or through the constitutive tethering of Gef1 to cell tips, and we biochemically demonstrate that the GAPs Rga3/6 and the GEF Gef1 are direct substrates of Sty1. We propose that phosphorylation of Rga3/6 and Gef1 mediates the Sty1-dependent inhibition of Cdc42 at cell tips, halting polarized growth during stress adaptation.Clàudia Salat-CanelaMercè CarmonaRebeca Martín-GarcíaPilar PérezJosé AytéElena HidalgoElsevierarticleSty1Cdc42cell polaritystress responsecell sizeGAPBiology (General)QH301-705.5ENCell Reports, Vol 37, Iss 5, Pp 109951- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Sty1 Cdc42 cell polarity stress response cell size GAP Biology (General) QH301-705.5
spellingShingle	Sty1 Cdc42 cell polarity stress response cell size GAP Biology (General) QH301-705.5 Clàudia Salat-Canela Mercè Carmona Rebeca Martín-García Pilar Pérez José Ayté Elena Hidalgo Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
description	Summary: Cdc42 GTPase rules cell polarity and growth in fission yeast. It is negatively and positively regulated by GTPase-activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), respectively. Active Cdc42-GTP localizes to the poles, where it associates with numerous proteins constituting the polarity module. However, little is known about its downregulation. We describe here that oxidative stress causes Sty1-kinase-dependent Cdc42 inactivation at cell poles. Both the amount of active Cdc42 at tips and cell length inversely correlate with Sty1 activity, explaining the elongated morphology of Δsty1 cells. We have created stress-blinded cell poles either by eliminating two Cdc42 GAPs or through the constitutive tethering of Gef1 to cell tips, and we biochemically demonstrate that the GAPs Rga3/6 and the GEF Gef1 are direct substrates of Sty1. We propose that phosphorylation of Rga3/6 and Gef1 mediates the Sty1-dependent inhibition of Cdc42 at cell tips, halting polarized growth during stress adaptation.
format	article
author	Clàudia Salat-Canela Mercè Carmona Rebeca Martín-García Pilar Pérez José Ayté Elena Hidalgo
author_facet	Clàudia Salat-Canela Mercè Carmona Rebeca Martín-García Pilar Pérez José Ayté Elena Hidalgo
author_sort	Clàudia Salat-Canela
title	Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
title_short	Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
title_full	Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
title_fullStr	Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
title_full_unstemmed	Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42
title_sort	stress-dependent inhibition of polarized cell growth through unbalancing the gef/gap regulation of cdc42
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/6387bfcfd2c149ada5f5a78fed45275b
work_keys_str_mv	AT claudiasalatcanela stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42 AT mercecarmona stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42 AT rebecamartingarcia stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42 AT pilarperez stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42 AT joseayte stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42 AT elenahidalgo stressdependentinhibitionofpolarizedcellgrowththroughunbalancingthegefgapregulationofcdc42
_version_	1718445275447558144

Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42

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