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Vol. 10, Issue 3, 581-596, March 1999
and
*Departments of Neurobiology and Cell Biology, University of
Alabama at Birmingham, Birmingham, Alabama 35294;
Recent cloning of a rat brain phosphatidylinositol
3,4,5-trisphosphate binding protein, centaurin Department of Molecular and Cell Biology, University of
California, Berkeley, California 94720-3202; Laboratory
of Molecular Signalling, Babraham Institute, Department of Zoology,
University of Cambridge, Cambridge, United Kingdom CB2 3ES;
§Department of Chemistry, State University of New York at
Stony Brook, Stony Brook, New York 11794; and Department
of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112
, identified a novel
gene family based on homology to an amino-terminal zinc-binding domain. In Saccharomyces cerevisiae, the protein with the
highest homology to centaurin is Gcs1p, the product of the
GCS1 gene. GCS1 was originally identified
as a gene conditionally required for the reentry of cells into the cell
cycle after stationary phase growth. Gcs1p was previously characterized
as a guanosine triphosphatase-activating protein for the small
guanosine triphosphatase Arf1, and gcs1 mutants
displayed vesicle-trafficking defects. Here, we have shown that similar
to centaurin , recombinant Gcs1p bound phosphoinositide-based affinity resins with high affinity and specificity. A novel
GCS1 disruption strain (gcs1
)
exhibited morphological defects, as well as mislocalization of cortical
actin patches. gcs1 was hypersensitive to the actin
monomer-sequestering drug, latrunculin-B. Synthetic lethality was
observed between null alleles of GCS1 and
SLA2, the gene encoding a protein involved in
stabilization of the actin cytoskeleton. In addition, synthetic growth
defects were observed between null alleles of GCS1 and
SAC6, the gene encoding the yeast fimbrin homologue.
Recombinant Gcs1p bound to actin filaments, stimulated actin
polymerization, and inhibited actin depolymerization in vitro. These
data provide in vivo and in vitro evidence that Gcs1p interacts
directly with the actin cytoskeleton in S. cerevisiae.
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