Document Detail


Ras and the Rho effector Cla4 collaborate to target and anchor Lte1 at the bud cortex.
MedLine Citation:
PMID:  15917658     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lte1, a protein important for exit from mitosis, localizes to the bud cortex as soon as the bud forms and remains there until cells exit from mitosis. Ras, the Rho GTPase Cdc42 and its effector the protein kinase Cla4 are required for Lte1's association with the bud cortex. Here we investigate how Ras, and the Cdc42 effector Cla4 regulate the localization of Lte1. We find that Ras2 and Lte1 associate in stages of the cell cycle when Lte1 is phosphorylated and associated with the bud cortex and that this association requires CLA4. Additionally, RAS1 and RAS2 are required for CLA4-dependent Lte1 phosphorylation. Our findings suggest that Cla4-dependent phosphorylation promotes the initial association of Lte1 with Ras at the bud cortex and that Ras is required to stabilize phosphorylated forms of Lte1 at the bud cortex. Our results also raise the interesting possibility that the localization of Lte1 affects the protein's ability to promote mitotic exit.
Authors:
Anupama Seshan; Angelika Amon
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2005-07-29
Journal Detail:
Title:  Cell cycle (Georgetown, Tex.)     Volume:  4     ISSN:  1551-4005     ISO Abbreviation:  Cell Cycle     Publication Date:  2005 Jul 
Date Detail:
Created Date:  2005-08-26     Completed Date:  2006-05-04     Revised Date:  2009-07-22    
Medline Journal Info:
Nlm Unique ID:  101137841     Medline TA:  Cell Cycle     Country:  United States    
Other Details:
Languages:  eng     Pagination:  940-6     Citation Subset:  IM    
Affiliation:
Center for Cancer Research, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenylate Cyclase / metabolism
Anaphase
Cell Cycle Proteins / metabolism
Gene Expression Regulation, Fungal
Guanine Nucleotide Exchange Factors / metabolism*
Phosphorylation
Protein Binding
Protein Transport
Protein Tyrosine Phosphatases / metabolism
Protein-Serine-Threonine Kinases / metabolism*
S Phase
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / metabolism*
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
ras Proteins / metabolism*
rho GTP-Binding Proteins / metabolism*
Grant Support
ID/Acronym/Agency:
GM 56800/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/CDC14 protein, S cerevisiae; 0/Cell Cycle Proteins; 0/Guanine Nucleotide Exchange Factors; 0/LTE1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; EC 2.7.11.1/CLA4 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 3.1.3.48/Protein Tyrosine Phosphatases; EC 3.6.5.2/RAS1 protein, S cerevisiae; EC 3.6.5.2/RAS2 protein, S cerevisiae; EC 3.6.5.2/cdc42 GTP-Binding Protein, Saccharomyces cerevisiae; EC 3.6.5.2/ras Proteins; EC 3.6.5.2/rho GTP-Binding Proteins; EC 4.6.1.1/Adenylate Cyclase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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