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Sla1p

Identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe, Sla1p is an organiser of the actin cytoskeleton and colocalises with actin patches. Sla1p is 136kDa (in S. cerevisiae), containing three SH3 domains at the N-terminus, a putative SH3 binding proline rich region at the central region and a series of  G, P, Q rich repeats in the C-terminal region similar to those found in another yeast actin regulating protein Pan1p, with which it forms a complex (Zeng et al, 2001).  Sla1p also binds End3p (Tang et al, 2000).

References:-

Tang, H. Y., Xu, J. & Cai, M. J. (2000) Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Mol.Cell Biol. 20, 12-25.

Warren, D. T., Andrews, P. D., Gourlay, C. W. & Ayscough, K. R. (2002) Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics.  J.Cell Biol. 115, 1703-1715.

Zeng, G., Yu, X. & Cai, M. (2001) Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p., Mol.Biol.Cell. 12, 3759-3773.

 
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