Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractTransport of organic environmental contaminants to animal products    Next AbstractUrinary biomonitoring of subjects with different smoking habits. Part I: Profiling mercapturic acids »

Mol Biol Cell


Title:Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation
Author(s):Friesen H; Murphy K; Breitkreutz A; Tyers M; Andrews B;
Address:"Department of Molecular and Medical Genetics, University of Toronto, Toronto, Canada, M5S 1A8"
Journal Title:Mol Biol Cell
Year:2003
Volume:20030404
Issue:7
Page Number:3027 - 3040
DOI: 10.1091/mbc.e02-09-0613
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"The yeast amphiphysin homologue Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. Rvs167p is a phosphoprotein in vegetatively growing cells and shows increased phosphorylation upon treatment with mating pheromone. Previous work has shown that Rvs167p can be phosphorylated in vitro by the cyclin-dependent kinase Pho85p complexed with its cyclin Pcl2p. Using chymotryptic phosphopeptide mapping, we have identified the sites on which Rvs167p is phosphorylated in vitro by Pcl2p-Pho85p. We have shown that these same sites are phosphorylated in vivo during vegetative growth and that phosphorylation at two of these sites is Pcl-Pho85p dependent. In cells treated with mating pheromone, the MAP kinase Fus3p is needed for full phosphorylation of Rvs167p. Functional genomics and genetics experiments revealed that mutation of other actin cytoskeleton genes compromises growth of a strain in which phosphorylation of Rvs167p is blocked by mutation. Phosphorylation of Rvs167p inhibits its interaction in vitro with Las17p, an activator of the Arp2/3 complex, as well as with a novel protein, Ymr192p. Our results suggest that phosphorylation of Rvs167p by a cyclin-dependent kinase and by a MAP kinase is an important mechanism for regulating protein complexes involved in actin cytoskeleton function"
Keywords:"Actin-Related Protein 2 Actin-Related Protein 3 Actins/metabolism Animals Cells, Cultured Cyclin-Dependent Kinases/*metabolism Cyclins/metabolism Cytoskeletal Proteins/metabolism Insect Viruses Microfilament Proteins Mitogen-Activated Protein Kinases/meta;"
Notes:"MedlineFriesen, Helena Murphy, Kelly Breitkreutz, Ashton Tyers, Mike Andrews, Brenda eng Research Support, Non-U.S. Gov't 2003/07/15 Mol Biol Cell. 2003 Jul; 14(7):3027-40. doi: 10.1091/mbc.e02-09-0613. Epub 2003 Apr 4"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 27-12-2024