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. |
