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PROSITE documentation PDOC00297 [for PROSITE entry PS51263]

ADF-H domain profile





Description

The actin-depolymerizing factor homology (ADF-H) domain is an ~150-amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins [1,2,3]:

  • ADF/cofilins, which include ADF, cofilin, destrin, actophorin, coactosin, depactin and glia maturation factors (GMFs) β and γ. ADF/cofilins are small actin-binding proteins composed of a single ADF-H domain. They bind both actin-monomers and filaments and promote rapid filament turnover in cells by depolymerizing/fragmenting actin filaments. ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin monomers.
  • Twinfilins. They are actin monomer-binding proteins that are composed of two ADF-H domains.
  • Abp1/Drebrins. They are relatively large proteins composed of an N-terminal ADF-H domain followed by a variable region and a C-terminal SH3 domain (see <PS50002>). Abp1/Drebrins interact only with actin filaments and do not promote filament depolymerization or fragmentation.

Although these proteins are biochemically distinct and play different roles in actin dynamics, they all appear to use the ADF-H domain for their interactions with actin.

The ADF-H domain consists of a six-stranded mixed β-sheet in which the four central strands (β2-β5) are anti-parallel and the two edge strands (β1 and β6) run parallel with the neighboring strands. The sheet is surrounded by two α-helices on each side (see <PDB:1COF>) [1,2,4].

The profile we developed covers the entire ADF-H domain.

Last update:

October 2006 / Pattern removed, profile added and text revised.

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Technical section

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

ADF_H, PS51263; ADF-H domain profile  (MATRIX)


References

1AuthorsLappalainen P. Kessels M.M. Cope M.J. Drubin D.G.
TitleThe ADF homology (ADF-H) domain: a highly exploited actin-binding module.
SourceMol. Biol. Cell 9:1951-1959(1998).
PubMed ID9693358

2AuthorsPaavilainen V.O. Merckel M.C. Falck S. Ojala P.J. Pohl E. Wilmanns M. Lappalainen P.
TitleStructural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin.
SourceJ. Biol. Chem. 277:43089-43095(2002).
PubMed ID12207032
DOI10.1074/jbc.M208225200

3AuthorsLiu L.X. Xu H. Weller P.F. Shi A. Debnath I.
TitleStructure and expression of a novel filarial gene for glia maturation factor.
SourceGene 186:1-5(1997).
PubMed ID9047337

4AuthorsLiu L. Wei Z. Wang Y. Wan M. Cheng Z. Gong W.
TitleCrystal structure of human coactosin-like protein.
SourceJ. Mol. Biol. 344:317-323(2004).
PubMed ID15522287
DOI10.1016/j.jmb.2004.09.036



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