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 AbstractEndocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes    Next AbstractInfluence of Methoprene on Pheromone Emission and Sexual Maturation of Anastrepha obliqua (Diptera: Tephritidae) males »

Mol Biol Cell


Title:"end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae"
Author(s):Munn AL; Stevenson BJ; Geli MI; Riezman H;
Address:"Department of Biochemistry, Biozentrum of the University of Basel, Switzerland"
Journal Title:Mol Biol Cell
Year:1995
Volume:6
Issue:12
Page Number:1721 - 1742
DOI: 10.1091/mbc.6.12.1721
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"Four mutants defective in endocytosis were isolated by screening a collection of temperature-sensitive yeast mutants. Three mutations define new END genes: end5-1, end6-1, and end7-1. The fourth mutation is in END4, a gene identified previously. The end5-1, end6-1, and end7-1 mutations do not affect vacuolar protein localization, indicating that the defect in each mutant is specific for internalization at the plasma membrane. Interestingly, localization of actin patches on the plasma membrane is affected in each of the mutants. end5-1, end6-1, and end7-1 are allelic to VRP1, RVS161, and ACT1, respectively. VRP1 and RVS161 are required for correct actin localization and ACT1 encodes actin. To our surprise, the end6-1 mutation fails to complement the act1-1 mutation. Disruption of the RVS167 gene, which is homologous to END6/RVS161 and which is also required for correct actin localization, also blocks endocytosis. The end7-1 mutant allele has a glycine 48 to aspartic acid substitution in the DNase I-binding loop of actin. We propose that Vrp1p, Rvs161p, and Rvs167p are components of a cytoskeletal structure that contains actin and fimbrin and that is required for formation of endocytic vesicles at the plasma membrane"
Keywords:"Actins/*biosynthesis/chemistry/genetics Alleles Amino Acid Sequence Base Sequence Biological Transport Chromosome Mapping Chromosomes, Fungal Crosses, Genetic *Cytoskeletal Proteins DNA Primers Endocytosis/genetics/physiology Fungal Proteins/*biosynthesis;"
Notes:"MedlineMunn, A L Stevenson, B J Geli, M I Riezman, H eng Comparative Study Research Support, Non-U.S. Gov't 1995/12/01 Mol Biol Cell. 1995 Dec; 6(12):1721-42. doi: 10.1091/mbc.6.12.1721"

 
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 25-11-2024