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Molecular and Cellular Biology, February 2001, p. 827-839, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.827-839.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Dynamic Localization and Function of Bni1p at the Sites of Directed Growth in Saccharomyces cerevisiae

Kumi Ozaki-Kuroda, Yasunori Yamamoto, Hidenori Nohara, Makoto Kinoshita, Takeshi Fujiwara, Kenji Irie, and Yoshimi Takai*

Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita, Osaka 565-0871, Japan

Received 1 September 2000/Returned for modification 20 October 2000/Accepted 7 November 2000

Formin homology (FH) proteins are implicated in cell polarization and cytokinesis through actin organization. There are two FH proteins in the yeast Saccharomyces cerevisiae, Bni1p and Bnr1p. Bni1p physically interacts with Rho family small G proteins (Rho1p and Cdc42p), actin, two actin-binding proteins (profilin and Bud6p), and a polarity protein (Spa2p). Here we analyzed the in vivo localization of Bni1p by using a time-lapse imaging system and investigated the regulatory mechanisms of Bni1p localization and function in relation to these interacting proteins. Bni1p fused with green fluorescent protein localized to the sites of cell growth throughout the cell cycle. In a small-budded cell, Bni1p moved along the bud cortex. This dynamic localization of Bni1p coincided with the apparent site of bud growth. A bni1-disrupted cell showed a defect in directed growth to the pre-bud site and to the bud tip (apical growth), causing its abnormally spherical cell shape and thick bud neck. Bni1p localization at the bud tips was absolutely dependent on Cdc42p, largely dependent on Spa2p and actin filaments, and partly dependent on Bud6p, but scarcely dependent on polarized cortical actin patches or Rho1p. These results indicate that Bni1p regulates polarized growth within the bud through its unique and dynamic pattern of localization, dependent on multiple factors, including Cdc42p, Spa2p, Bud6p, and the actin cytoskeleton.

* Corresponding author. Mailing address: Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, 2-2 Yamada-Oka, Suita, Osaka 565-0871, Japan. Phone: 81-6-6879-3410. Fax: 81-6-6879-3419. E-mail: ytakai{at}molbio.med.osaka-u.ac.jp.

Molecular and Cellular Biology, February 2001, p. 827-839, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.827-839.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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