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PROSITE documentation PDOC51072 [for PROSITE entry PS51072]

Mu homology domain (MHD) profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

MHD, PS51072; Mu homology domain (MHD) profile  (MATRIX)


References

1AuthorsMartina J.A. Bonangelino C.J. Aguilar R.C. Bonifacino J.S.
TitleStonin 2: an adaptor-like protein that interacts with components of the endocytic machinery.
SourceJ. Cell Biol. 153:1111-1120(2001).
PubMed ID11381094

2AuthorsWalther K. Krauss M. Diril M.K. Lemke S. Ricotta D. Honing S. Kaiser S. Haucke V.
TitleHuman stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating.
SourceEMBO Rep. 2:634-640(2001).
PubMed ID11454741
DOI10.1093/embo-reports/kve134

3AuthorsWalther K. Diril M.K. Jung N. Haucke V.
TitleFunctional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin.
SourceProc. Natl. Acad. Sci. U.S.A. 101:964-969(2004).
PubMed ID14726597
DOI10.1073/pnas.0307862100

4AuthorsReider A. Barker S.L. Mishra S.K. Im Y.J. Maldonado-Baez L. Hurley J.H. Traub L.M. Wendland B.
TitleSyp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.
SourceEMBO J. 28:3103-3116(2009).
PubMed ID19713939
DOI10.1038/emboj.2009.248

5AuthorsOwen D.J. Evans P.R.
TitleA structural explanation for the recognition of tyrosine-based endocytotic signals.
SourceScience 282:1327-1332(1998).
PubMed ID9812899



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