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Vol. 10, Issue 4, 1061-1075, April 1999
and
*Department of Biochemistry, University of Dundee, Dundee DD1 5EH,
Scotland, United Kingdom; and SLA1 was identified previously in budding yeast in a
genetic screen for mutations that caused a requirement for the
actin-binding protein Abp1p and was shown to be required for normal
cortical actin patch structure and organization. Here, we show that
Sla1p, like Abp1p, localizes to cortical actin patches. Furthermore, Sla1p is required for the correct localization of Sla2p, an
actin-binding protein with homology to talin implicated in endocytosis,
and the Rho1p-GTPase, which is associated with the cell wall
biosynthesis enzyme Department of Molecular
and Cell Biology, University of California, Berkeley, California 94720
-1,3-glucan synthase. Mislocalization of Rho1p
in sla1 null cells is consistent with our observation
that these cells possess aberrantly thick cell walls. Expression
of mutant forms of Sla1p in which specific domains were deleted showed
that the phenotypes associated with the full deletion are functionally separable. In particular, a region of Sla1p encompassing the third SH3
domain is important for growth at high temperatures, for the organization of cortical actin patches, and for nucleated actin assembly in a permeabilized yeast cell assay. The apparent redundancy between Sla1p and Abp1p resides in the C-terminal repeat region of
Sla1p. A homologue of SLA1 was identified in
Schizosaccharomyces pombe. Despite relatively low
overall sequence homology, this gene was able to rescue the temperature
sensitivity associated with a deletion of SLA1 in
Saccharomyces cerevisiae.
Corresponding author. E-mail address:
kayscough{at}bad.dundee.ac.uk.
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