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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2006
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v103_n11_p4116_Aguilar http://hdl.handle.net/20.500.12110/paper_00278424_v103_n11_p4116_Aguilar |
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paper:paper_00278424_v103_n11_p4116_Aguilar2023-06-08T14:54:21Z Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins Actin Endocytosis Polarity clathrin epsin guanosine triphosphatase activating protein phosphatidylinositide protein Cdc42 scaffold protein amino terminal sequence article cell polarity endocytosis ENT1 gene ENT2 gene fungal gene nonhuman priority journal protein domain protein protein interaction sequence homology yeast Adaptor Proteins, Signal Transducing Carrier Proteins cdc42 GTP-Binding Protein, Saccharomyces cerevisiae Cell Polarity Endocytosis Genes, Fungal Models, Molecular Mutation Phenotype Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Eukaryota 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 ent1Δent2Δ 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. © 2006 by The National Academy of Sciences of the USA. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v103_n11_p4116_Aguilar http://hdl.handle.net/20.500.12110/paper_00278424_v103_n11_p4116_Aguilar |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Actin Endocytosis Polarity clathrin epsin guanosine triphosphatase activating protein phosphatidylinositide protein Cdc42 scaffold protein amino terminal sequence article cell polarity endocytosis ENT1 gene ENT2 gene fungal gene nonhuman priority journal protein domain protein protein interaction sequence homology yeast Adaptor Proteins, Signal Transducing Carrier Proteins cdc42 GTP-Binding Protein, Saccharomyces cerevisiae Cell Polarity Endocytosis Genes, Fungal Models, Molecular Mutation Phenotype Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Eukaryota |
| spellingShingle |
Actin Endocytosis Polarity clathrin epsin guanosine triphosphatase activating protein phosphatidylinositide protein Cdc42 scaffold protein amino terminal sequence article cell polarity endocytosis ENT1 gene ENT2 gene fungal gene nonhuman priority journal protein domain protein protein interaction sequence homology yeast Adaptor Proteins, Signal Transducing Carrier Proteins cdc42 GTP-Binding Protein, Saccharomyces cerevisiae Cell Polarity Endocytosis Genes, Fungal Models, Molecular Mutation Phenotype Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Eukaryota Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| topic_facet |
Actin Endocytosis Polarity clathrin epsin guanosine triphosphatase activating protein phosphatidylinositide protein Cdc42 scaffold protein amino terminal sequence article cell polarity endocytosis ENT1 gene ENT2 gene fungal gene nonhuman priority journal protein domain protein protein interaction sequence homology yeast Adaptor Proteins, Signal Transducing Carrier Proteins cdc42 GTP-Binding Protein, Saccharomyces cerevisiae Cell Polarity Endocytosis Genes, Fungal Models, Molecular Mutation Phenotype Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Eukaryota |
| description |
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 ent1Δent2Δ 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. © 2006 by The National Academy of Sciences of the USA. |
| title |
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| title_short |
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| title_full |
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| title_fullStr |
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| title_full_unstemmed |
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins |
| title_sort |
epsin n-terminal homology domains perform an essential function regulating cdc42 through binding cdc42 gtpase-activating proteins |
| publishDate |
2006 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v103_n11_p4116_Aguilar http://hdl.handle.net/20.500.12110/paper_00278424_v103_n11_p4116_Aguilar |
| _version_ |
1768544444635676672 |