The Tea4-PP1 landmark promotes local growth by dual Cdc42 GEF recruitment and GAP exclusion.
Details
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State: Public
Version: Final published version
State: Public
Version: Final published version
Serval ID
serval:BIB_74CC809F3679
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The Tea4-PP1 landmark promotes local growth by dual Cdc42 GEF recruitment and GAP exclusion.
Journal
Journal of Cell Science
ISSN
1477-9137 (Electronic)
ISSN-L
0021-9533
Publication state
Published
Issued date
2014
Volume
127
Number
Pt 9
Pages
2005-2016
Language
english
Abstract
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.
Keywords
Cdc42, Schizosaccharomyces pombe, Cell polarization, Type I phosphatase, Tea4, PP1
Pubmed
Web of science
Open Access
Yes
Create date
15/04/2014 20:43
Last modification date
20/08/2019 15:32