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Li, R (1997) Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136:649-58

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 delta bee1 cells form aberrant bundles that do not contain most of the cortical cytoskeletal components. It is significant that delta 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.

PubMed PMC2134298

Actins/metabolism; Actins/physiology; Base Sequence; Carrier Proteins/metabolism; Cell Division/physiology; Cytoskeletal Proteins; Cytoskeleton/metabolism; Cytoskeleton/physiology; DNA, Fungal; Fungal Proteins/genetics; Fungal Proteins/metabolism; Gene Deletion; Golgi Apparatus/metabolism; Humans; Molecular Sequence Data; Proteins/chemistry; Saccharomyces cerevisiae Proteins; Wiskott-Aldrich Syndrome/metabolism; Wiskott-Aldrich Syndrome Protein; src Homology Domains