Document Detail


Secretion is required for late events in the cell-fusion pathway of mating yeast.
MedLine Citation:
PMID:  20460435     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Secretory vesicles accumulate adjacent to the contact site between the two cells of a yeast mating pair before they fuse, but there is no direct evidence that secretion is required to complete fusion. In this study, temperature-sensitive secretion (sec(ts)) mutants were used to investigate the role of secretion in yeast cell fusion. Cell fusion arrested less than 5 minutes after inhibiting secretion. This rapid fusion arrest was not an indirect consequence of reduced mating pheromone signaling, mating-pair assembly or actin polarity. Furthermore, secretion was required to complete cell fusion when it was transiently inhibited by addition and removal of the lipophilic styryl dye, FM4-64. These results indicate that ongoing secretion is required for late events in the cell-fusion pathway, which include plasma-membrane fusion and the completion of cell-wall remodeling, and they demonstrate a just-in-time delivery mechanism for the cell-fusion machinery.
Authors:
Eric Grote
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-05-11
Journal Detail:
Title:  Journal of cell science     Volume:  123     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-20     Completed Date:  2010-09-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1902-12     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, 615 N. Wolfe Street, Baltimore, MD 21205. egrote@jhsph.edu
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MeSH Terms
Descriptor/Qualifier:
Cells, Cultured
Genetic Complementation Test
Membrane Fusion / drug effects,  genetics
Membrane Proteins / genetics
Mutation / genetics
Pyridinium Compounds / pharmacology
Quaternary Ammonium Compounds / pharmacology
Reproduction
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Secretory Pathway
Secretory Vesicles / metabolism*
Temperature
Vesicular Transport Proteins / genetics,  metabolism*
Yeasts / physiology*
beta-Galactosidase / metabolism*
Chemical
Reg. No./Substance:
0/FM 4-64; 0/FUS1 protein, S cerevisiae; 0/Membrane Proteins; 0/PRM1 protein, S cerevisiae; 0/Pyridinium Compounds; 0/Quaternary Ammonium Compounds; 0/SEC6 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Vesicular Transport Proteins; EC 3.2.1.23/beta-Galactosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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