PROSITE documentation PDOC51072Mu homology domain (MHD) profile
The mu homology domain (MHD) is an ~280 residue protein-protein interaction module, which is found in endocytotic proteins involved in clathrin-mediated endocytosis [1,2,3,4]:
- Mu subunits of adaptor protein (AP) complexes, AP-1, AP-2, AP-3, and AP-4 (see <PDOC00761>).
- Proteins of the stonin family.
- Proteins of the muniscin family: Syp1, FCHO1/2 and SGIP1.
The MHD domain has an elongated, banana-shaped, all β-sheet structure (see <PDB:1BW8>). It can be considered as two β-sandwich subdomains (A and B), with subdomain B inserted between strands 6 and 15 of subdomain A, and joined edge to edge such that the convex surface is a continuous nine-stranded mixed β-sheet that runs the whole length of the molecule. The tyrosine based signal binds to a site on the surface of two parallel β-sheet strands (β1 and β16) in subdomain A [4,5].
The profile we developed covers the entire MHD domain.
Last update:October 2013 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Martina J.A. Bonangelino C.J. Aguilar R.C. Bonifacino J.S. |
| Title | Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery. | |
| Source | J. Cell Biol. 153:1111-1120(2001). | |
| PubMed ID | 11381094 |
| 2 | Authors | Walther K. Krauss M. Diril M.K. Lemke S. Ricotta D. Honing S. Kaiser S. Haucke V. |
| Title | Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating. | |
| Source | EMBO Rep. 2:634-640(2001). | |
| PubMed ID | 11454741 | |
| DOI | 10.1093/embo-reports/kve134 |
| 3 | Authors | Walther K. Diril M.K. Jung N. Haucke V. |
| Title | Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 101:964-969(2004). | |
| PubMed ID | 14726597 | |
| DOI | 10.1073/pnas.0307862100 |
| 4 | Authors | Reider A. Barker S.L. Mishra S.K. Im Y.J. Maldonado-Baez L. Hurley J.H. Traub L.M. Wendland B. |
| Title | Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. | |
| Source | EMBO J. 28:3103-3116(2009). | |
| PubMed ID | 19713939 | |
| DOI | 10.1038/emboj.2009.248 |
| 5 | Authors | Owen D.J. Evans P.R. |
| Title | A structural explanation for the recognition of tyrosine-based endocytotic signals. | |
| Source | Science 282:1327-1332(1998). | |
| PubMed ID | 9812899 |
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