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Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2006 Mar 14; Vol. 103 (11), pp. 4116-21. Date of Electronic Publication: 2006 Mar 06. - Publication Year :
- 2006
-
Abstract
- Epsins are endocytic proteins with a structured epsin N-terminal homology (ENTH) domain that binds phosphoinositides and a poorly structured C-terminal region that interacts with ubiquitin and endocytic machinery, including clathrin and endocytic scaffolding proteins. Yeast has two redundant genes encoding epsins, ENT1 and ENT2; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of ent1Deltaent2Delta cells. Mutational analysis of the ENTH domain revealed a surface patch that is essential for viability and that binds guanine nucleotide triphosphatase-activating proteins for Cdc42, a critical regulator of cell polarity in all eukaryotes. Furthermore, the epsins contribute to regulation of specific Cdc42 signaling pathways in yeast cells. These data support a model in which the epsins function as spatial and temporal coordinators of endocytosis and cell polarity.
- Subjects :
- Adaptor Proteins, Signal Transducing genetics
Adaptor Proteins, Vesicular Transport
Carrier Proteins genetics
Cell Polarity
Endocytosis
Genes, Fungal
Models, Molecular
Mutation
Phenotype
Protein Structure, Tertiary
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins genetics
Vesicular Transport Proteins
Adaptor Proteins, Signal Transducing chemistry
Adaptor Proteins, Signal Transducing metabolism
Carrier Proteins chemistry
Carrier Proteins metabolism
Saccharomyces cerevisiae Proteins chemistry
Saccharomyces cerevisiae Proteins metabolism
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 103
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 16537494
- Full Text :
- https://doi.org/10.1073/pnas.0510513103