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Molecular and Cellular Biology, November 2002, p. 7889-7906, Vol. 22, No. 22
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.22.7889-7906.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Saccharomyces cerevisiae Bzz1p Is Implicated with Type I Myosins in Actin Patch Polarization and Is Able To Recruit Actin-Polymerizing Machinery In Vitro

Alexandre Soulard,1 Terry Lechler,2 Vladislav Spiridonov,1 Andrej Shevchenko,3 Anna Shevchenko,3 Rong Li,2 and Barbara Winsor1*

Modèles levure des Pathologies Humaines, F.R.E. 2375 du Centre National de la Recheche Scientifique, Strasbourg, France,1 Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115,2 Max Planck Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany3

Received 15 May 2002/ Returned for modification 19 June 2002/ Accepted 19 August 2002

In Saccharomyces cerevisiae, the WASP (Wiskott-Aldrich syndrome protein) homologue Las17p (also called Bee1p) is an important component of cortical actin patches. Las17p is part of a high-molecular-weight protein complex that regulates Arp2/3 complex-dependent actin polymerization at the cell cortex and that includes the type I myosins Myo3p and Myo5p and verprolin (Vrp1p). To identify other factors implicated with this complex in actin regulation, we isolated proteins that bind to Las17p by two-hybrid screening and affinity chromatography. Here, we report the characterization of Lsb7/Bzz1p (for Las seventeen binding protein 7), an Src homology 3 (SH3) domain protein that interacts directly with Las17p via a polyproline-SH3 interaction. Bzz1p coimmunoprecipitates in a complex with Las17p, Vrp1p, Myo3/5p, Bbc1p, Hsp70p, and actin. It colocalizes with cortical actin patches and with Las17p. This localization is dependent on Las17p, but not on F-actin. Bzz1p interacts physically and genetically with type I myosins. While deletion of BZZ1 shows no obvious phenotype, simultaneous deletion of the BZZ1, MYO3, and MYO5 genes is lethal. Overexpression of Bzz1p inhibits cell growth, and a bzz1{Delta} myo5{Delta} double mutant is unable to restore actin polarity after NaCl stress. Finally, Bzz1p in vitro is able to recruit a functional actin polymerization machinery through its SH3 domains. Its interactions with Las17p, Vrp1p, and the type I myosins are essential for this process. This suggests that Bzz1p could be implicated in the regulation of actin polymerization.

* Corresponding author. Mailing address: Institut de Biologie Moléculaire et Cellulaire du C.N.R.S. F.R.E. 2375, Modèles d'Etude des Pathologies Humaines, 15 Rue Descartes, 67084 Strasbourg, France. Phone: 33 (0)3 90 24 14 70. Fax: 33 (0)3 88 41 7070. E-mail: B.Winsor{at}ibmc.u-strasbg.fr.

Molecular and Cellular Biology, November 2002, p. 7889-7906, Vol. 22, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.22.7889-7906.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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