InterPro domain: IPR014712

The AP180 N-terminal homology (ANTH) domain is a membrane binding domain found in endocytotic accessory proteins, such as AP180. The ANTH domain is involved in phosphatidylinositol 4,5-bisphosphate (also known as PIP2) binding and is also responsible for membrane localisation of AP180. The ANTH domain containing proteins appear to be universal elements in nucleation of clathrin coats [ 1 , 2 ].

The N-terminal phosphoinositide-binding domain of CALM and AP180 consist of nine alpha helices forming a solenoid structure. This is most similar to the ENTH domain of epsin, with the first seven helices of epsin superimposing well on those of CALM. However, in epsin the final alpha8 helix folds back across the others, whereas in CALM and AP180 the final three long helices continue the solenoidal pattern [ 3 ].

1. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. 278, 28993-9
2. ENTH/ANTH domains expand to the Golgi. Trends Cell Biol. 13, 211-5
3. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 291, 1051-5