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 AbstractThe role of vision in odor-plume tracking by walking and flying insects    Next AbstractUrea additions and defoliation affect plant responses to elevated CO(2) in a C(3) grass from Yellowstone National Park »

EMBO J


Title:"Vps1p, a member of the dynamin GTPase family, is necessary for Golgi membrane protein retention in Saccharomyces cerevisiae"
Author(s):Wilsbach K; Payne GS;
Address:"Molecular Biology Institute, University of California, Los Angeles 90024"
Journal Title:EMBO J
Year:1993
Volume:12
Issue:8
Page Number:3049 - 3059
DOI: 10.1002/j.1460-2075.1993.tb05974.x
ISSN/ISBN:0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking)
Abstract:"The KEX2-encoded endoprotease of Saccharomyces cerevisiae resides in the Golgi complex where it participates in the maturation of alpha-factor mating pheromone precursor. Clathrin heavy chain gene disruptions cause mislocalization of Kex2p to the cell surface and reduce maturation of the alpha-factor precursor. Based on these findings, a genetic screen has been devised to isolate mutations that affect retention of Kex2p in the Golgi complex. Two alleles of a single genetic locus, lam1 (lowered alpha-factor maturation), have been isolated, which result in inefficient maturation of alpha-factor precursor. In lam1 cells, Kex2p is not mislocalized to the cell surface but is abnormally unstable. Normal stability is restored by the pep4 mutation which reduces the activity of vacuolar proteases. In contrast, the pheromone maturation defect is not corrected by pep4. Organelle fractionation by sucrose density gradient centrifugation shows that Kex2p is not retained in the Golgi complex of lam1 cells. Vacuolar protein precursors are secreted by lam1 mutants, revealing another sorting defect in the Golgi complex. Genetic complementation reveals that lam1 is allelic to the VPS1 gene, which encodes a dynamin-related GTPase. These results indicate that Vps1p is necessary for membrane protein retention in a late Golgi compartment"
Keywords:Alleles Biological Transport Carrier Proteins/*metabolism GTP Phosphohydrolases/*metabolism *GTP-Binding Proteins Genetic Complementation Test Golgi Apparatus/*metabolism Mating Factor Membrane Proteins/*metabolism Mutation Peptides/genetics/metabolism *P;
Notes:"MedlineWilsbach, K Payne, G S eng GM 07185/GM/NIGMS NIH HHS/ GM 39040/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 1993/08/01 EMBO J. 1993 Aug; 12(8):3049-59. doi: 10.1002/j.1460-2075.1993.tb05974.x"

 
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 26-06-2024