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 AbstractSome nutritional characteristics of predominant culturable ruminal bacteria    Next AbstractThe prevalence of Cowdria ruminantium in free-living adult Amblyomma hebraeum collected at a communal grazing area and in 2 wildlife reserves in South Africa »

Eur J Cell Biol


Title:"Traffic into the prevacuolar/endosomal compartment of Saccharomyces cerevisiae: a VPS45-dependent intracellular route and a VPS45-independent, endocytic route"
Author(s):Bryant NJ; Piper RC; Gerrard SR; Stevens TH;
Address:"Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA"
Journal Title:Eur J Cell Biol
Year:1998
Volume:76
Issue:1
Page Number:43 - 52
DOI: 10.1016/S0171-9335(98)80016-2
ISSN/ISBN:0171-9335 (Print) 0171-9335 (Linking)
Abstract:"The vps (vacuolar protein sorting) mutants have been used to dissect and characterize the vacuolar biogenesis pathway in the yeast Saccharomyces cerevisiae. The vps mutants were isolated through their loss of ability to correctly sort the vacuolar hydrolase CPY, which travels from Golgi membranes to the vacuole through a prevacuolar compartment. Over 50 VPS genes have been divided into 6 classes according to vacuolar morphology. Mutations in any one of the class E VPS genes, such as VPS27, lead to an exaggerated form of the prevacuolar compartment. This class E compartment contains endocytosed proteins as well as proteins en route to the vacuole, and is thus taken to represent an intersection point between the endocytic and biosynthetic pathways. Mutations in the class D gene VPS45 can be used to define a second transport intermediate along the vacuolar biogenesis pathway, Golgi-derived transport vesicles carrying vacuolar membrane proteins on their way to the vacuole. Here we demonstrate that the Sec1p-like protein Vps45p is required for the fusion of Golgi-derived vesicles with the prevacuolar compartment indicating that VPS45 functions before VPS27 in the vacuolar biogenesis pathway. In addition, we show that VPS45 function is not required for the delivery of endocytosed proteins to the prevacuolar compartment from the plasma membrane suggesting that the function of Vps45p is restricted to a single vesicular pathway"
Keywords:"Biological Transport Carboxypeptidases/metabolism Carrier Proteins/genetics/metabolism Cathepsin A Cell Compartmentation Endocytosis Endosomes/*metabolism Epistasis, Genetic Fungal Proteins/genetics/*metabolism *GTP-Binding Proteins Membrane Proteins/gene;"
Notes:"MedlineBryant, N J Piper, R C Gerrard, S R Stevens, T H eng GM16601/GM/NIGMS NIH HHS/ GM32448/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. Germany 1998/07/03 Eur J Cell Biol. 1998 May; 76(1):43-52. doi: 10.1016/S0171-9335(98)80016-2"

 
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 26-12-2024