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 Abstract[Determination of volatile organic compounds in drinking water by purge and trap gas chromatography/mass spectrometry]    Next AbstractNovel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant »

Traffic


Title:"An ER membrane protein, Sop4, facilitates ER export of the yeast plasma membrane [H+]ATPase, Pma1"
Author(s):Luo WJ; Gong XH; Chang A;
Address:"Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, New York 10461, USA"
Journal Title:Traffic
Year:2002
Volume:3
Issue:10
Page Number:730 - 739
DOI: 10.1034/j.1600-0854.2002.31005.x
ISSN/ISBN:1398-9219 (Print) 1398-9219 (Linking)
Abstract:"We have analyzed the mechanism by which Sop4, a novel ER membrane protein, regulates quality control and intracellular transport of Pma1-7, a mutant plasma membrane ATPase. At the restrictive temperature, newly synthesized Pma1-7 is targeted for vacuolar degradation instead of being correctly delivered to the cell surface. Loss of Sop4 at least partially corrects vacuolar mislocalization, allowing Pma1-7 routing to the plasma membrane. Ste2-3 is a mutant pheromone receptor which, like Pma1-7, is defective in targeting to the cell surface, resulting in a mating defect. sop4delta suppresses the mating defect of ste2-3 cells as well as the growth defect of pma1-7. Visualization of newly synthesized Pma1-7 in sop4delta cells by indirect immunofluorescence reveals delayed export from the ER. Similarly, ER export of wild-type Pma1 is delayed in the absence of Sop4 although intracellular transport of Gas1 and CPY is unaffected. These observations suggest a model in which a selective increase in ER residence time for Pma1-7 may allow it to achieve a more favorable conformation for subsequent delivery to the plasma membrane. In support of this model, newly synthesized Pma1-7 is also routed to the plasma membrane upon release from a general block of ER-to-Golgi transport in sec13-1 cells"
Keywords:"Base Sequence DNA Primers Endoplasmic Reticulum/*metabolism Fungal Proteins/genetics/*metabolism Genes, Suppressor Protein Transport Proton-Translocating ATPases/*metabolism Saccharomyces cerevisiae Proteins/*metabolism;"
Notes:"MedlineLuo, Wen-jie Gong, Xiao-hua Chang, Amy eng GM58212/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. England 2002/09/17 Traffic. 2002 Oct; 3(10):730-9. doi: 10.1034/j.1600-0854.2002.31005.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 19-12-2024