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J. Biol. Chem., Vol. 283, Issue 22, 14988-14993, May 30, 2008

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The Caenorhabditis elegans AMP-activated Protein Kinase AAK-2 Is Phosphorylated by LKB1 and Is Required for Resistance to Oxidative Stress and for Normal Motility and Foraging Behavior^*

Hyojin Lee¹, Jeong Soo Cho¹, Nils Lambacher, Jieun Lee, Se-Jin Lee, Tae Hoon Lee, Anton Gartner, and Hyeon-Sook Koo²

From the Department of Biochemistry, College of Science, Yonsei University, Seoul 120-749, Korea and the Wellcome Trust Centre for Gene Regulation and Expression, School of Life Sciences, The University of Dundee, Dow Street, Dundee DD1 5EH Scotland, United Kingdom

AAK-2 is one of two isoforms of the AMP-activated protein kinase in Caenorhabditis elegans and is involved in life span maintenance, stress responses, and germ cell cycle arrest upon dauer entry. We found that AAK-2 was phosphorylated at threonine 243 in response to paraquat treatment and that this phosphorylation depends on PAR-4, the C. elegans LKB1 homologue. Both aak-2 mutation and par-4 knockdown increased the sensitivity of C. elegans worms to paraquat, and the double deficiency did not further increase sensitivity, indicating that aak-2 and par-4 act in a linear pathway. Both mutations also slowed body bending during locomotion and failed to reduce head oscillation in response to anterior touch. Consistent with this abnormal motility and behavioral response, expression of the AAK-2::green fluorescent protein fusion protein was observed in the ventral cord, some neurons, body wall muscle, pharynx, vulva, somatic gonad, and excretory cell. Our study suggests that AMPK can influence the behavior of C. elegans worms in addition to its well known function in metabolic control.

Received for publication, November 6, 2007 , and in revised form, April 4, 2008.

^* This work was supported by Korea Research Foundation Grant KRF-2005-041-C00305 funded by the Korean Government (Ministry of Education and Human Resources Development) (to H.-S. K.) and by a Cancer Research United Kingdom Career Development Award fellowship (to A. G.). 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–S3.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 822-2123-2701; Fax: 822-362-9897; E-mail: kooh{at}yonsei.ac.kr.

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