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InterPro: IPR016365 Actobindin
Protein matches
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UniProtKB Matches: 5 proteins |
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Accession
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IPR016365 Actobindin |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR003124 Actin-binding WH2
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This group represents an actobindin; a 9.8kDa protein from Acanthamoeba castellanii [1]. It belongs to a group of G-actin binding proteins including actobindin, twinfilin, and profilin [2]. Actobindin consists of two beta-thymosin repeats [3]. It inhibits nucleation of new actin filaments and facilitates elongation of existing polarized filaments in actively motile regions [4]. Actobindin does not form a stable complex with actin dimers but causes the accumulation of dimers that are unable to nucleate polymerisation or self-associate [5].
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Publications
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1.
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Bubb MR, Lewis MS, Korn ED.
Actobindin binds with high affinity to a covalently cross-linked actin dimer.
J. Biol. Chem. 269 25587-91 1994
[PubMed: 7929261]
http://intl.jbc.org/cgi/reprint/269/41/25587.pdf
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2.
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Arasada R, Gloss A, Tunggal B, Joseph JM, Rieger D, Mondal S, Faix J, Schleicher M, Noegel AA.
Profilin isoforms in Dictyostelium discoideum.
Biochim. Biophys. Acta 1773 631-41 2007
[PubMed: 17467078]
http://dx.doi.org/10.1016/j.bbamcr.2007.03.009
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3.
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Hertzog M, Yarmola EG, Didry D, Bubb MR, Carlier MF.
Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family.
J. Biol. Chem. 277 14786-92 2002
[PubMed: 11856744]
http://dx.doi.org/10.1074/jbc.M112064200
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4.
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Bubb MR, Baines IC, Korn ED.
Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acanthamoeba castellanii.
Cell Motil. Cytoskeleton 39 134-46 1998
[PubMed: 9484955]
http://dx.doi.org/10.1002/(SICI)1097-0169(1998)39:2<134::AID-CM4>3.0.CO;2-6
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5.
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Bubb MR, Knutson JR, Porter DK, Korn ED.
Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate.
J. Biol. Chem. 269 25592-7 1994
[PubMed: 7929262]
http://intl.jbc.org/cgi/reprint/269/41/25592.pdf
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InterPro 24.0
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