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J. Biol. Chem., Vol. 281, Issue 37, 27090-27098, September 15, 2006

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Direct Phosphorylation and Activation of a Nim1-related Kinase Gin4 by Elm1 in Budding Yeast^*

Satoshi Asano¹, Jung-Eun Park¹, Li-Rong Yu, Ming Zhou, Krisada Sakchaisri, Chong J. Park, Young H. Kang, Jeremy Thorner^¶, Timothy D. Veenstra, and Kyung S. Lee²

From the Laboratory of Metabolism, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892, the Laboratory of Proteomics and Analytical Technologies, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702, and the ^¶Department of Molecular and Cell Biology, University of California, Berkeley, California 94720

In budding yeast, Gin4, a Nim1-related kinase, plays an important role in proper organization of the septin ring at the mother-bud neck, a filamentous structure that is critical for diverse cellular processes including mitotic entry and cytokinesis. How Gin4 kinase activity is regulated is not known. Here we showed that a neck-associated Ser/Thr kinase Elm1, which is important for septin assembly, is critical for proper modification of Gin4 and its physiological substrate Shs1. In vitro studies with purified recombinant proteins demonstrated that Elm1 directly phosphorylates and activates Gin4, which in turn phosphorylates Shs1. Consistent with these observations, acute inhibition of Elm1 activity abolished mitotic Gin4 phosphorylation and Gin4-dependent Shs1 modification in vivo. In addition, a gin4 mutant lacking the Elm1-dependent phosphorylation sites exhibited an impaired localization to the bud-neck and, as a result, induced a significant growth defect with an elongated bud morphology. Thus, Elm1 regulates the septin assembly-dependent cellular events by directly phosphorylating and activating the Gin4-dependent pathway(s).

Received for publication, February 15, 2006 , and in revised form, July 17, 2006.

^* This work was supported in part by a NCI/National Institutes of Health intramural grant (to K. S. L.) and a National Institutes of Health Grant GM21841 (to J. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ The first two authors contributed equally to this work.

² To whom correspondence should be addressed: NCI, National Institutes of Health, 9000 Rockville Pike, Bldg. 37, Rm. 3118, Bethesda, MD 20892. Tel.: 301-496-9635; Fax: 301-496-8419; E-mail: kyunglee{at}mail.nih.gov.

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