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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.

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



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