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 AbstractOn-line coupling of equilibrium-sorptive enrichment to gas chromatography to determine low-molecular-mass pollutants in environmental water samples    Next AbstractStructure of sterol aliphatic chains affects yeast cell shape and cell fusion during mating »

Mol Biol Cell


Title:The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating
Author(s):Aguilar PS; Engel A; Walter P;
Address:"Howard Hughes Medical Institute, and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA. pablo.aguilar@ucsf.edu"
Journal Title:Mol Biol Cell
Year:2007
Volume:20061206
Issue:2
Page Number:547 - 556
DOI: 10.1091/mbc.e06-09-0776
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"As for most cell-cell fusion events, the molecular details of membrane fusion during yeast mating are poorly understood. The multipass membrane protein Prm1 is the only known component that acts at the step of bilayer fusion. In its absence, mutant mating pairs lyse or arrest in the mating reaction with tightly apposed plasma membranes. We show that deletion of FIG 1, which controls pheromone-induced Ca(2+) influx, yields similar cell fusion defects. Although extracellular Ca(2+) is not required for efficient cell fusion of wild-type cells, cell fusion in prm1 mutant mating pairs is dramatically reduced when Ca(2+) is removed. This enhanced fusion defect is due to lysis. Time-lapse microscopy reveals that fusion and lysis events initiate with identical kinetics, suggesting that both outcomes result from engagement of the fusion machinery. The yeast synaptotagmin orthologue and Ca(2+) binding protein Tcb3 has a role in reducing lysis of prm1 mutants, which opens the possibility that the observed role of Ca(2+) is to engage a wound repair mechanism. Thus, our results suggest that Prm1 and Fig1 have a role in enhancing membrane fusion and maintaining its fidelity. Their absence results in frequent mating pair lysis, which is counteracted by Ca(2+)-dependent membrane repair"
Keywords:Cytoplasm/chemistry/physiology Egtazic Acid/pharmacology Fungal Proteins/analysis/genetics/*physiology *Membrane Fusion Membrane Proteins/analysis/genetics/*physiology Synaptotagmins/physiology Yeasts/chemistry/drug effects/*physiology;
Notes:"MedlineAguilar, Pablo S Engel, Alex Walter, Peter eng Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't 2006/12/08 Mol Biol Cell. 2007 Feb; 18(2):547-56. doi: 10.1091/mbc.e06-09-0776. Epub 2006 Dec 6"

 
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 27-12-2024