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פותח על ידי קלירמאש פתרונות בע"מ -
A Mechanism for Cell-Cycle Regulation of MAP Kinase Signaling in a Yeast Differentiation Pathway
Year:
2007
Source of publication :
Cell
Authors :
בן-ארי, גיורא
;
.
Volume :
128
Co-Authors:
Strickfaden, S.C., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Winters, M.J., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Ben-Ari, G., Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, M5G 1X5, Canada
Lamson, R.E., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Tyers, M., Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, M5G 1X5, Canada, Department of Medical Genetics and Microbiology, University of Toronto, Toronto, M5S 1A8, Canada
Pryciak, PeterM., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Facilitators :
From page:
519
To page:
531
(
Total pages:
13
)
Abstract:
Yeast cells arrest in the G1 phase of the cell cycle upon exposure to mating pheromones. As cells commit to a new cycle, G1 CDK activity (Cln/CDK) inhibits signaling through the mating MAPK cascade. Here we show that the target of this inhibition is Ste5, the MAPK cascade scaffold protein. Cln/CDK disrupts Ste5 membrane localization by phosphorylating a cluster of sites that flank a small, basic, membrane-binding motif in Ste5. Effective inhibition of Ste5 signaling requires multiple phosphorylation sites and a substantial accumulation of negative charge, which suggests that Ste5 acts as a sensor for high G1 CDK activity. Thus, Ste5 is an integration point for both external and internal signals. When Ste5 cannot be phosphorylated, pheromone triggers an aberrant arrest of cells outside G1 either in the presence or absence of the CDK-inhibitor protein Far1. These findings define a mechanism and physiological benefit of restricting antiproliferative signaling to G1. © 2007 Elsevier Inc. All rights reserved.
Note:
Related Files :
cell membrane
Cell Proliferation
protein localization
Saccharomyces cerevisiae Proteins
unclassified drug
Yeast
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.cell.2006.12.032
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29556
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:47
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Scientific Publication
A Mechanism for Cell-Cycle Regulation of MAP Kinase Signaling in a Yeast Differentiation Pathway
128
Strickfaden, S.C., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Winters, M.J., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Ben-Ari, G., Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, M5G 1X5, Canada
Lamson, R.E., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
Tyers, M., Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, M5G 1X5, Canada, Department of Medical Genetics and Microbiology, University of Toronto, Toronto, M5S 1A8, Canada
Pryciak, PeterM., Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605, United States
A Mechanism for Cell-Cycle Regulation of MAP Kinase Signaling in a Yeast Differentiation Pathway
Yeast cells arrest in the G1 phase of the cell cycle upon exposure to mating pheromones. As cells commit to a new cycle, G1 CDK activity (Cln/CDK) inhibits signaling through the mating MAPK cascade. Here we show that the target of this inhibition is Ste5, the MAPK cascade scaffold protein. Cln/CDK disrupts Ste5 membrane localization by phosphorylating a cluster of sites that flank a small, basic, membrane-binding motif in Ste5. Effective inhibition of Ste5 signaling requires multiple phosphorylation sites and a substantial accumulation of negative charge, which suggests that Ste5 acts as a sensor for high G1 CDK activity. Thus, Ste5 is an integration point for both external and internal signals. When Ste5 cannot be phosphorylated, pheromone triggers an aberrant arrest of cells outside G1 either in the presence or absence of the CDK-inhibitor protein Far1. These findings define a mechanism and physiological benefit of restricting antiproliferative signaling to G1. © 2007 Elsevier Inc. All rights reserved.
Scientific Publication
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