The ENTH domain |
| |
Authors: | De Camilli Pietro Chen Hong Hyman Joel Panepucci Ezequiel Bateman Alex Brunger Axel T |
| |
Institution: | Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA. pietro.decamilli@yale.edu |
| |
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. |
| |
Keywords: | VHS domain Ubiquitin Clathrin AP-2 Endocytosis EH domain |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|