title: The ENTH domain.
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.
authors.affiliation: Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA. pietro.decamilli@yale.edu
authors.forename: Pietro
authors.initials: P
authors.lastname: De Camilli
authors.forename: Hong
authors.initials: H
authors.lastname: Chen
authors.forename: Joel
authors.initials: J
authors.lastname: Hyman
authors.forename: Ezequiel
authors.initials: E
authors.lastname: Panepucci
authors.forename: Alex
authors.initials: A
authors.lastname: Bateman
authors.forename: Axel T
authors.initials: AT
authors.lastname: Brunger
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D016384:Consensus Sequence; D008565:Membrane Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D008565:Membrane Proteins; D025801:Ubiquitin