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Department of Cell Biology, Harvard Medical School, Boston, MA 02115
Yeast protein, Bee1, exhibits sequence homology to Wiskott-Aldrich syndrome protein (WASP),
a human protein that may link signaling pathways to
the actin cytoskeleton. Mutations in WASP are the primary cause of Wiskott-Aldrich syndrome, characterized by immuno-deficiencies and defects in blood cell
morphogenesis. This report describes the characterization of Bee1 protein function in budding yeast. Disruption of BEE1 causes a striking change in the organization of actin filaments, resulting in defects in budding
and cytokinesis. Rather than assemble into cortically associated patches, actin filaments in the buds of 
bee1
cells form aberrant bundles that do not contain most of
the cortical cytoskeletal components. It is significant
that bee1 is the only mutation reported so far that
abolishes cortical actin patches in the bud. Bee1 protein
is localized to actin patches and interacts with Sla1p, a
Src homology 3 domain-containing protein previously implicated in actin assembly and function. Thus, Bee1
protein may be a crucial component of a cytoskeletal
complex that controls the assembly and organization of
actin filaments at the cell cortex.
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