ANTH domain explained

The ANTH domain is a membrane binding domain that shows weak specificity for PtdIns(4,5)P2. It was found in AP180 (homologous to CALM[1]) endocytotic accessory protein that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.[2] [3]

Its structure is a solenoid of 9 helices. The PtdIns(4,5)P2 binding residues are spread over several helices at the tip of the structure. The PtdIns(4,5)P2 binding sequence is Kx9Kx(K/R)(H/Y).

An ANTH domain is also found in HIP1 and HIP1R, and the PtdIns(4,5)P2 binding sequence is conserved.

Human proteins containing this domain

HIP1

HIP1R; PICALM; SNAP91;

Further reading

External links

Notes and References

  1. Web site: Clathrin and its interactions with AP180. https://web.archive.org/web/20070311024540/http://www.endocytosis.org/AP180/Clathrin.html. 2007-03-11.
  2. de Camilli P, McMahon HT, Peter BJ, Stahelin RV, Cho W, Long F, Murray D . Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains . J. Biol. Chem. . 278 . 31 . 28993–9 . 2003 . 12740367 . 10.1074/jbc.M302865200. free .
  3. Payne GS, Duncan MC . ENTH/ANTH domains expand to the Golgi . Trends Cell Biol. . 13 . 5 . 211–5 . 2003 . 12742163 . 10.1016/S0962-8924(03)00076-X.