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© The Rockefeller University Press, 0021-9525/1997//649 $5.00
The Journal of Cell Biology, Volume 136, Number 3, , 1997 649-658

Article

Bee1, a Yeast Protein with Homology to Wiscott-Aldrich Syndrome Protein, Is Critical for the Assembly of Cortical Actin Cytoskeleton



Rong Li

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 {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.

Abbreviations used in this paper: Bee1p, Bee1 protein; GBD, GTPasebinding domain; SH3, Src homology 3; WAS, Wiskott-Aldrich syndrome; WASP, Wiskott-Aldrich syndrome protein; WH1, WASP homology domain 1.

I am very grateful to Tom Kirchhausen for communicating the sequence similarity between Bee1p and WASP before its publication and for his encouragement throughout these studies. I am indebted to David Drubin, John Cooper, and John Pringle for generously providing antibodies. I am grateful to Susanna Rankin and Le Ma for their help in light microscopy, and Maria Ericsson for her expert assistance in electron microscopy. I am grateful to the members of my laboratory, and Dan Sun and Tika Li for support and encouragement. I thank Christine Field, Dan Finley, Ryn Miake-Lye, Tim Mitchison, David Pellman, Tom Rapaport, and Dirk Winter for their comments on the manuscript.

Address all correspondence to Rong Li, Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115. Tel: (617) 432-0640. Fax: (617) 432-1144. E-mail: RLi{at}warren.med.harvard.edu


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