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PROSITE documentation PDOC51089 [for PROSITE entry PS51089]

Headpiece (HP) domain profile





Description

Headpiece is an ~70-residue F-actin-binding domain present at the C terminus of many cytoskeletal proteins [1]. It was first discovered in the epithelial brush border protein villin, a member of the gelsolin family, which consists of six gelsolin repeats, followed by the C-terminal headpiece domain [2].

The headpiece domain folds in a very compact globular structure organized around an extended hydrophobic core (see <PDB:1QQV>) [1]. It is composed of a highly α-helical C-terminal subdomain and an N-terminal subdomain made up of bends and turns with a short α-helix. Most of the actin-binding residues identified by biochemical studies are localized on a single face on the surface of the domain [3].

Some of the proteins known to contain a headpiece domain are listed below:

  • Eukaryotic villin protein, a Ca(2+)-regulated actin-binding protein. Villin has been demonstrated to bundle and sever F-actin [4].
  • Drosophila villin-like protein quail.
  • Vertebrate dematin, an actin-bundling protein.
  • Animal actin-binding LIM (AbLIM) or limatin protein. It may act as scaffold protein and may play a role in axon guidance.
  • Vertebrate advillin protein. It may function in the morphogenesis of neuronal cells which form ganglia.
  • Supervillin protein. It forms a high-affinity link between the actin cytoskeleton and the membrane.

The profile we developed covers the whole headpiece domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

March 2005 / First entry.

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Technical section

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

HP, PS51089; Headpiece (HP) domain profile  (MATRIX)


References

1AuthorsVardar D. Buckley D.A. Frank B.S. McKnight C.J.
TitleNMR structure of an F-actin-binding 'headpiece' motif from villin.
SourceJ. Mol. Biol. 294:1299-1310(1999).
PubMed ID10600386
DOI10.1006/jmbi.1999.3321

2AuthorsFinidori J. Friederich E. Kwiatkowski D.J. Louvard D.
TitleIn vivo analysis of functional domains from villin and gelsolin.
SourceJ. Cell Biol. 116:1145-1155(1992).
PubMed ID1310994

3AuthorsVermeulen W. Vanhaesebrouck P. Van Troys M. Verschueren M. Fant F. Goethals M. Ampe C. Martins J.C. Borremans F.A.
TitleSolution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements.
SourceProtein Sci. 13:1276-1287(2004).
PubMed ID15096633
DOI10.1110/ps.03518104

4AuthorsBretscher A. Weber K.
TitleVillin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.
SourceCell 20:839-847(1980).
PubMed ID6893424



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

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