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).
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.
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.