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 AbstractMutation of the SPS1-encoded protein kinase of Saccharomyces cerevisiae leads to defects in transcription and morphology during spore formation    Next Abstract"An LC-MS/MS method to profile urinary mercapturic acids, metabolites of electrophilic intermediates of occupational and environmental toxicants" »

Mol Biol Cell


Title:Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo
Author(s):Friesen H; Humphries C; Ho Y; Schub O; Colwill K; Andrews B;
Address:"Department of Medical Genetics and Microbiology, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5S 1A8"
Journal Title:Mol Biol Cell
Year:2006
Volume:20060104
Issue:3
Page Number:1306 - 1321
DOI: 10.1091/mbc.e05-06-0476
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"We have used comprehensive synthetic lethal screens and biochemical assays to examine the biological role of the yeast amphiphysin homologues Rvs161p and Rvs167p, two proteins that play a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. We found that unlike some forms of amphiphysin, Rvs161p-Rvs167p acts as an obligate heterodimer during vegetative growth and neither Rvs161p nor Rvs167p forms a homodimer in vivo. RVS161 and RVS167 have an identical set of 49 synthetic lethal interactions, revealing functions for the Rvs proteins in cell polarity, cell wall synthesis, and vesicle trafficking as well as a shared role in mating. Consistent with these roles, we show that the Rvs167p-Rvs161p heterodimer, like its amphiphysin homologues, can bind to phospholipid membranes in vitro, suggesting a role in vesicle formation and/or fusion. Our genetic screens also reveal that the interaction between Abp1p and the Rvs167p Src homology 3 (SH3) domain may be important under certain conditions, providing the first genetic evidence for a role for the SH3 domain of Rvs167p. Our studies implicate heterodimerization of amphiphysin family proteins in various functions related to cell polarity, cell integrity, and vesicle trafficking during vegetative growth and the mating response"
Keywords:"Actins/metabolism Animals Carrier Proteins/metabolism Cattle Cell Line Cell Membrane/metabolism Chitin/metabolism Cytoskeletal Proteins/*chemistry/*metabolism Dimerization Diploidy Gene Deletion Genes, Mating Type, Fungal Genetic Complementation Test Inse;"
Notes:"MedlineFriesen, Helena Humphries, Christine Ho, Yuen Schub, Oliver Colwill, Karen Andrews, Brenda eng Research Support, Non-U.S. Gov't 2006/01/06 Mol Biol Cell. 2006 Mar; 17(3):1306-21. doi: 10.1091/mbc.e05-06-0476. Epub 2006 Jan 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 17-11-2024