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Domain binding and function: The EH domain is a module of ~100 amino acids originally identified in the tyrosine kinase substrate Eps15, and thus termed the Eps15-Homology (EH) domain. There is considerable evidence to suggest that EH domain proteins are primarily involved in regulating endocytosis and vesicle transport. Typically, EH domains recognize peptides with core NPF motifs. Most EH proteins have multiple copies of the EH domain, and may bind cooperatively to proteins with several NPF motifs. EH domain proteins frequently have other repeated motifs (i.e., DPF, PXXP, coiled-coil) and modules (i.e., SH3 domains), suggesting that they may serve a scaffolding function in endocytosis. Indeed, the DPF motifs of Eps15 interact with the N-terminal appendage region of the clathrin adaptor AP-2 component, alpha-Adaptin. Eps15, and other EH domain proteins such as Intersectin, can bind proteins implicated in endocytosis, such as the GTPase Dynamin and the lipid phosphatase Synaptojanin. Genetic data in yeast have directly demonstrated the importance of an EH domain protein, Pan1, in endocytosis.
Structure Reference: De Beer, T. et al. (1998) Science 281(5381), 1357À1360.
Examples of Domain Proteins:
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| The central EH domain of Eps15. | |
