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PMID: 8380177 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae.

The Journal of cell biology ·Vol. 120 ·No. 1 ·1993-01-00 ·Pages 55-65

Raths S, Rohrer J, Crausaz F, Riezman H

Abstract

alpha-factor, one of two peptide hormones responsible for synchronized mating between MATa and MAT alpha-cell types in Saccharomyces cerevisiae, binds to its cell surface receptor and is internalized in a time-, temperature-, and energy-dependent manner (Chvatchko, Y., I. Howald, and H. Riezman. 1986. Cell. 46:355-364). After internalization, alpha-factor is delivered to the vacuole via vesicular intermediates and degraded there consistent with an endocytic mechanism (Singer, B., and H. Riezman. 1990. J. Cell Biol. 110:1911-1922; Chvatchko, Y., I. Howald, and H. Riezman. 1986. Cell. 46:355-364). We have isolated two mutants that are defective in the internalization process. Both mutations confer a recessive, temperature-sensitive growth phenotype upon cells that cosegregates with their endocytosis defect. Lucifer yellow, a marker for fluid-phase endocytosis, shows accumulation characteristics in the mutants that are similar to the uptake characteristics of 35S-alpha-factor. The endocytic defect in end4 cells appears immediately upon shift to restrictive temperature and is reversible at permissive temperature if new protein synthesis is allowed. Furthermore, the end4 mutation only affects alpha-factor internalization and not the later delivery of alpha-factor to the vacuole. Other vesicle-mediated processes seem to be normal in end3 and end4 mutants. END3 and END4 are the first genes shown to be necessary for the internalization step of receptor-borne and fluid-phase markers in yeast.

Related Genes
END3 END4
MeSH Terms
Carboxypeptidases/metabolism Cathepsin A Down-Regulation Endocytosis Fungal Proteins/metabolism Genes, Fungal Glycoside Hydrolases/metabolism Mating Factor Mutagenesis Peptides/metabolism Receptors, Cell Surface/metabolism Receptors, Mating Factor Receptors, Peptide Saccharomyces cerevisiae/physiology Saccharomyces cerevisiae Proteins Temperature Transcription Factors beta-Fructofuranosidase
Chemicals
Fungal Proteins Peptides Receptors, Cell Surface Receptors, Mating Factor Receptors, Peptide Saccharomyces cerevisiae Proteins Transcription Factors Mating Factor Glycoside Hydrolases beta-Fructofuranosidase Carboxypeptidases Cathepsin A PRC1 protein, S cerevisiae serine carboxypeptidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Raths S
Biocenter, University of Basel, Switzerland.
Rohrer J
Crausaz F
Riezman H
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.120.1.55
Published
1993-01-00
Pages
55-65
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2119492
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.120.1.55 PMC Full Text View journal details
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