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PMID: 10330397 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum.

The Journal of cell biology ·Vol. 145 ·No. 4 ·1999-05-17 ·Pages 659-72

Roberg KJ, Crotwell M, Espenshade P, Gimeno R, Kaiser CA

Abstract

In Saccharomyces cerevisiae, vesicles that carry proteins from the ER to the Golgi compartment are encapsulated by COPII coat proteins. We identified mutations in ten genes, designated LST (lethal with sec-thirteen), that were lethal in combination with the COPII mutation sec13-1. LST1 showed synthetic-lethal interactions with the complete set of COPII genes, indicating that LST1 encodes a new COPII function. LST1 codes for a protein similar in sequence to the COPII subunit Sec24p. Like Sec24p, Lst1p is a peripheral ER membrane protein that binds to the COPII subunit Sec23p. Chromosomal deletion of LST1 is not lethal, but inhibits transport of the plasma membrane proton-ATPase (Pma1p) to the cell surface, causing poor growth on media of low pH. Localization by both immunofluorescence microscopy and cell fractionation shows that the export of Pma1p from the ER is impaired in lst1Delta mutants. Transport of other proteins from the ER was not affected by lst1Delta, nor was Pma1p transport found to be particularly sensitive to other COPII defects. Together, these findings suggest that a specialized form of the COPII coat subunit, with Lst1p in place of Sec24p, is used for the efficient packaging of Pma1p into vesicles derived from the ER.

MeSH Terms
Amino Acid Sequence Biological Transport COP-Coated Vesicles Cell Membrane/enzymology Endoplasmic Reticulum/metabolism Fungal Proteins/genetics,metabolism GTPase-Activating Proteins Membrane Proteins/genetics,metabolism Molecular Sequence Data Mutagenesis Phenotype Proton-Translocating ATPases/metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins
Chemicals
Fungal Proteins GTPase-Activating Proteins Membrane Proteins PMA2 protein, S cerevisiae SEC23 protein, S cerevisiae SEC24 protein, S cerevisiae SFB3 protein, S cerevisiae Saccharomyces cerevisiae Proteins PMA1 protein, S cerevisiae Proton-Translocating ATPases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Roberg K J
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Crotwell M
Espenshade P
Gimeno R
Kaiser C A
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.145.4.659
Published
1999-05-17
Pages
659-72
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2133178
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.145.4.659 PMC Full Text View journal details
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