Abstract

The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module composed by a superhelix of alpha-helices. It is present at the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors, and therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signaling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is structurally similar to the VHS domain. These domains define two families of adaptor proteins which function in membrane traffic and whose interaction with membranes is regulated, in part, by phosphoinositides.

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Cite this paper

@article{Camilli2002TheED, title={The ENTH domain.}, author={Pietro De Camilli and Hong Chen and Joel Hyman and Ezequiel Panepucci and Alex Bateman and Axel T Brunger}, journal={FEBS letters}, year={2002}, volume={513 1}, pages={11-8} }