Cell Signaling Technology

ENTH Domain

The ENTH domain of rat Epsin1.

Domain Binding and Function

First identified in the endocytotic protein epsin 1, the epsin NH2-terminal homology (ENTH) domain is a membrane binding motif of approximately 150 amino acids. Proteins containing this domain have been shown to bind to phospholipids including PtdIns(4,5)P2 and PtdIns(1,4,5)P3. Consistent with these findings, the primary function suggested for the ENTH domain containing proteins is to act as clathrin adaptors in endocytosis, with binding of the ENTH domain to the phospholipid bilayer allowing recruitment of clathrin components and clathrin accessory factors to the cell membrane. In addition, two ENTH containing proteins (HIP1, HIP1R), shown to localize to clathrin coated pits, also contain a putative actin binding motif (ILWEQ) providing evidence for the elusive link between the actin cytoskeleton and endocytosis.

Structure Reference

  1. Hyman, J. et.al. (2000) J. Cell Biol. 149(3), 537–46.

Examples of Domain Proteins

Binding Examples

ENTH Domain Proteins Binding Partners
Epsin1 PtdIns(4,5)P2 / PtdIns(1,4,5)P3
AP180 PtdIns(4,5)P2 / PtdIns(1,4,5)P3

Reference