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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Publicado: 2006
Materias:
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
Genes, Fungal
Models, Molecular
Mutation
Phenotype
Protein Structure, Tertiary
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Eukaryota
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
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

Ejemplares similares