Epsin N-Terminal Homology Domains Perform an Essential Function Regulating Cdc42 through Binding Cdc42 GTPase-Activating Proteins

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 e...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2006-03, Vol.103 (11), p.4116-4121
Main Authors: Aguilar, Rubén C., Longhi, Silvia A., Shaw, Jonathan D., Yeh, Lan-Yu, Kim, Sean, Schön, Arne, Freire, Ernesto, Hsu, Ariel, McCormick, William K., Watson, Hadiya A., Wendland, Beverly
Format: Article
Language:English
Subjects:
Actins
Adaptor Proteins, Signal Transducing - chemistry
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Adaptor Proteins, Vesicular Transport
Binding sites
Biological Sciences
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae - metabolism
Cell growth
Cell Polarity
Cellular biology
Endocytosis
Gene expression regulation
Genes, Fungal
HeLa cells
Models, Molecular
Mutation
Phenotype
Phenotypes
Plasmids
Protein Structure, Tertiary
Proteins
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Signal transduction
Vesicular Transport Proteins
Viability
Yeast
Yeasts
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Summary: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 entlΔent2Δ 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0510513103