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PMID: 15192110 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast.

The Journal of biological chemistry ·Vol. 279 ·No. 35 ·2004-08-27 ·Pages 36962-71

Aronov S, Gerst JE

Abstract

Both the delivery of secretory vesicles and asymmetric distribution of mRNA to the bud are dependent upon the actin cytoskeleton in yeast. Here we examined whether components of the exocytic apparatus play a role in mRNA transport. By screening secretion mutants in situ and in vivo, we found that all had an altered pattern of ASH1 mRNA localization. These included alleles of CDC42 and RHO3 (cdc42-6 and rho3-V51) thought to regulate specifically the fusion of secretory vesicles but were found to affect strongly the cytoskeleton as well. Most interestingly, mutations in late secretion-related genes not directly involved in actin regulation also showed substantial alterations in ASH1 mRNA distribution. These included mutations in genes encoding components of the exocyst (SEC10 and SEC15), SNARE regulatory proteins (SEC1, SEC4, and SRO7), SNAREs (SEC9 and SSO1/2), and proteins involved in Golgi export (PIK1 and YPT31/32). Importantly, prominent defects in the actin cytoskeleton were observed in all of these strains, thus implicating a known causal relationship between the deregulation of actin and the inhibition of mRNA transport. Our novel observations suggest that vesicular transport regulates the actin cytoskeleton in yeast (and not just vice versa) leading to subsequent defects in mRNA transport and localization.

MeSH Terms
Actins/chemistry,metabolism Alleles Binding Sites Biological Transport Cytoskeleton/metabolism Fungal Proteins/metabolism GTP Phosphohydrolases/metabolism Genes, Fungal Genotype Green Fluorescent Proteins Image Processing, Computer-Assisted In Situ Hybridization, Fluorescence Luminescent Proteins/metabolism Microscopy, Confocal Microscopy, Fluorescence Mutation Plasmids/metabolism RNA, Messenger/metabolism Temperature Yeasts/metabolism cdc42 GTP-Binding Protein, Saccharomyces cerevisiae/metabolism
Chemicals
Actins Fungal Proteins Luminescent Proteins RNA, Messenger Green Fluorescent Proteins GTP Phosphohydrolases cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Aronov Stella
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Gerst Jeffrey E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2004-08-27
Epub
2004-00-10
Pages
36962-71
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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