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PMID: 8730101 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast.

Molecular biology of the cell ·Vol. 7 ·No. 4 ·1996-04-00 ·Pages 579-94

Becherer KA, Rieder SE, Emr SD, Jones EW

Abstract

pep12/vps6 mutants of Saccharomyces cerevisiae are defective in delivery of soluble vacuolar hydrolases to the vacuole. Morphological analysis by electron microscopy revealed that pep12 cells accumulate 40- to 50-nm vesicles. Furthermore, pep12 cells have enlarged vacuoles characteristic of class D pep/vps mutants. PEP12 encodes a protein of 288 amino acids that has a C-terminal hydrophobic region and shares significant sequence similarity with members of the syntaxin protein family. These proteins appear to participate in the docking and fusion of intracellular transport vesicles. Pep12p is the first member of the syntaxin family to be implicated in transport between the Golgi and the vacuole/lysosome. Pep12p-specific polyclonal antisera detected a 35-kDa protein that fractionated as an integral membrane protein. Subcellular fractionation experiments revealed that Pep12p was associated with membrane fractions of two different densities; the major pool (approximately 90%) of pep12p may associate with the endosome, while a minor pool (approximately 10%) cofractionated with the late Golgi marker Kex2p. These observations suggest that Pep12p may mediate the docking of Golgi-derived transport vesicles at the endosome.

MeSH Terms
Amino Acid Sequence Animals Centrifugation, Density Gradient Cloning, Molecular Conserved Sequence Endosomes/chemistry,metabolism Fungal Proteins/chemistry,genetics,metabolism Gene Deletion Hydrolases/metabolism Membrane Proteins/chemistry,genetics,metabolism Molecular Sequence Data Phenotype Qa-SNARE Proteins Rats Saccharomyces cerevisiae/enzymology,ultrastructure Saccharomyces cerevisiae Proteins Vacuoles/enzymology
Chemicals
Fungal Proteins Membrane Proteins PEP12 protein, S cerevisiae Qa-SNARE Proteins SSO1 protein, S cerevisiae Saccharomyces cerevisiae Proteins Sed5 protein, S cerevisiae Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Becherer K A
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Rieder S E
Emr S D
Jones E W
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.7.4.579
Published
1996-04-00
Pages
579-94
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC275911
Subset
IM
Grants
NCI NIH HHS · CA-68589 · United States
NIGMS NIH HHS · GM-29713 · United States
NIGMS NIH HHS · GM-32703 · United States
Databases
GENBANK
M90395
External Links
PubMed source DOI: 10.1091/mbc.7.4.579 PMC Full Text View journal details
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