The Tea4-PP1 landmark promotes local growth by dual Cdc42 GEF recruitment and GAP exclusion.

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Ressource 1Télécharger: BIB_74CC809F3679.P001.pdf (5948.15 [Ko])
Etat: Serval
Version: Final published version
ID Serval
serval:BIB_74CC809F3679
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The Tea4-PP1 landmark promotes local growth by dual Cdc42 GEF recruitment and GAP exclusion.
Périodique
Journal of Cell Science
Auteur(s)
Kokkoris K., Gallo Castro D., Martin S.G.
ISSN
1477-9137 (Electronic)
ISSN-L
0021-9533
Statut éditorial
Publié
Date de publication
2014
Volume
127
Numéro
Pt 9
Pages
2005-2016
Langue
anglais
Résumé
Cell polarization relies on small GTPases, such as Cdc42, which can break symmetry through self-organizing principles, and landmarks that define the axis of polarity. In fission yeast, microtubules deliver the Tea1-Tea4 complex to mark cell poles for growth, but how this complex activates Cdc42 is unknown. Here, we show that ectopic targeting of Tea4 to cell sides promotes the local activation of Cdc42 and cell growth. This activity requires that Tea4 binds the type I phosphatase (PP1) catalytic subunit Dis2 or Sds21, and ectopic targeting of either catalytic subunit is similarly instructive for growth. The Cdc42 guanine-nucleotide-exchange factor Gef1 and the GTPase-activating protein Rga4 are required for Tea4-PP1-dependent ectopic growth. Gef1 is recruited to ectopic Tea4 and Dis2 locations to promote Cdc42 activation. By contrast, Rga4 is locally excluded by Tea4, and its forced colocalization with Tea4 blocks ectopic growth, indicating that Rga4 must be present, but at sites distinct from Tea4. Thus, a Tea4-PP1 landmark promotes local Cdc42 activation and growth both through Cdc42 GEF recruitment and by creating a local trough in a Cdc42 GAP.
Mots-clé
Cdc42, Schizosaccharomyces pombe, Cell polarization, Type I phosphatase, Tea4, PP1
Pubmed
Web of science
Open Access
Oui
Création de la notice
15/04/2014 20:43
Dernière modification de la notice
08/05/2019 20:28
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