The mitotic exit network regulates the spatiotemporal activity of Cdc42 to maintain cell size.
Anaphase
/ drug effects
Bridged Bicyclo Compounds, Heterocyclic
/ pharmacology
Cell Cycle Checkpoints
/ drug effects
Cell Cycle Proteins
/ metabolism
Cell Size
/ drug effects
Guanosine Triphosphate
/ metabolism
Metaphase
/ drug effects
Mitosis
/ drug effects
Nocodazole
/ pharmacology
Phosphorylation
/ drug effects
Protein Domains
Protein Tyrosine Phosphatases
/ metabolism
Saccharomyces cerevisiae
/ cytology
Saccharomyces cerevisiae Proteins
/ metabolism
Spindle Apparatus
/ drug effects
Thiazolidines
/ pharmacology
Time Factors
cdc42 GTP-Binding Protein
/ metabolism
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
04 01 2021
04 01 2021
Historique:
received:
05
01
2020
revised:
29
09
2020
accepted:
29
10
2020
entrez:
7
12
2020
pubmed:
8
12
2020
medline:
19
5
2021
Statut:
ppublish
Résumé
During G1 in budding yeast, the Cdc42 GTPase establishes a polar front, along which actin is recruited to direct secretion for bud formation. Cdc42 localizes at the bud cortex and then redistributes between mother and daughter in anaphase. The molecular mechanisms that terminate Cdc42 bud-localized activity during mitosis are poorly understood. We demonstrate that the activity of the Cdc14 phosphatase, released through the mitotic exit network, is required for Cdc42 redistribution between mother and bud. Induced Cdc14 nucleolar release results in premature Cdc42 redistribution between mother and bud. Inhibition of Cdc14 causes persistence of Cdc42 bud localization, which perturbs normal cell size and spindle positioning. Bem3, a Cdc42 GAP, binds Cdc14 and is dephosphorylated at late anaphase in a Cdc14-dependent manner. We propose that Cdc14 dephosphorylates and activates Bem3 to allow Cdc42 inactivation and redistribution. Our results uncover a mechanism through which Cdc14 regulates the spatiotemporal activity of Cdc42 to maintain normal cell size at cytokinesis.
Identifiants
pubmed: 33284320
pii: 211575
doi: 10.1083/jcb.202001016
pmc: PMC7721911
pii:
doi:
Substances chimiques
Bridged Bicyclo Compounds, Heterocyclic
0
CDC14 protein, S cerevisiae
0
Cell Cycle Proteins
0
Saccharomyces cerevisiae Proteins
0
Thiazolidines
0
Guanosine Triphosphate
86-01-1
Protein Tyrosine Phosphatases
EC 3.1.3.48
cdc42 GTP-Binding Protein
EC 3.6.5.2
latrunculin B
LW7U308U7U
Nocodazole
SH1WY3R615
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM105755
Pays : United States
Informations de copyright
© 2020 Gihana et al.
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