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Co-operation with the ADF/Cofilin.

The actin-binding protein AIP1 is known to enhance the activity of the ADF/Cofilins. Presently, this is the only protein (apart from the kinase/phosphatases) whose action synergizes with the ADF/Cofilin family.
 

References:-

Aizawa, H., Katadae, M., Maruya, M., Sameshima, M., Murakami-Murofushi, K. & Yahara, I. (1999) Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin., Genes to Cells. 4, 311-324.

Amberg, D. C., Basart, E. & Botstein, D. (1995) Defining protein interactions with yeast actin in vivo., Nature Struct. Biol. 2, 28-35.

Iida, K. & Yahara, I. (1999) Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharmyces cerevisiae., Genes to Cells. 4, 21-32.

 Jin, H. & Amberg, D. C. (2001) Fission yeast Aip3p (spAip3p) is required for an alternative actin-directed polarity program., Mol.Biol.Cell. 12, 1275-1291.

Okada, K., Obinata, T. & Abe, H. (1999) XAIP1: a Xenopus homoloque of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins., J.Cell Sci. 112, 1553-1565.

Ono, S. (2001) The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments., J.Cell Sci. 152, 1313-1319.

Rodal, A. A., Tetreault, J. W., Lappalainen, P., Drubin, D. G. & Amberg, D. C. (1999) Aip1p interacts with cofilin to disassemble actin filaments., J.Cell Biol. 145, 1251-1264.

 
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