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PMID: 7841519 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast.

Molecular biology of the cell ·Vol. 5 ·No. 9 ·1994-09-00 ·Pages 1023-37

Bénédetti H, Raths S, Crausaz F, Riezman H

Abstract

Two Saccharomyces cerevisiae mutants, end3 and end4, defective in the internalization step of endocytosis, have previously been isolated. The END3 gene was cloned by complementation of the temperature-sensitive growth defect caused by the end3 mutation and the END3 nucleotide sequence was determined. The END3 gene product is a 40-kDa protein that has a putative EF-hand Ca(2+)-binding site, a consensus sequence for the binding of phosphotidylinositol 4,5-bisphosphate (PIP2), and a C-terminal domain containing two homologous regions of 17-19 aa. The EF-hand consensus and the putative PIP2-binding sites are seemingly not required for End3 protein function. In contrast, different portions of the End3p N-terminal domain, and at least one of the two repeated regions in its C-terminus, are required for End3p activity. Disruption of the END3 gene yielded cells with the same phenotype as the original end3 mutant. An end3ts allele was obtained and this allowed us to demonstrate that End3p is specifically involved in the internalization step of endocytosis. In addition, End3p was shown to be required for proper organization of the actin cytoskeleton and for the correct distribution of chitin at the cell surface.

Related Genes
END3 end3 end4
MeSH Terms
Actin Cytoskeleton/ultrastructure Actins/metabolism Alleles Amino Acid Sequence Base Sequence Binding Sites Calcium/metabolism Chitin/metabolism Cloning, Molecular Cytoskeletal Proteins Cytoskeleton/ultrastructure Endocytosis/genetics Fungal Proteins/chemistry,genetics,physiology Genes, Fungal Molecular Sequence Data Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates/metabolism Point Mutation Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae/genetics,physiology,ultrastructure Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Deletion Sequence Homology, Amino Acid Structure-Activity Relationship Subcellular Fractions/chemistry
Chemicals
Actins Cytoskeletal Proteins END3 protein, S cerevisiae Fungal Proteins Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates Saccharomyces cerevisiae Proteins Chitin Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bénédetti H
Biozentrum of the University of Basel, Switzerland.
Raths S
Crausaz F
Riezman H
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.5.9.1023
Published
1994-09-00
Pages
1023-37
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC301124
Subset
IM
Databases
GENBANK
X79473
External Links
PubMed source DOI: 10.1091/mbc.5.9.1023 PMC Full Text View journal details
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