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J. Biol. Chem., Vol. 283, Issue 8, 4799-4807, February 22, 2008

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AMP-activated Protein Kinase Subunit Interactions

β1:1 ASSOCIATION REQUIRES β1 Thr-263 AND Tyr-267^*

Tristan J. Iseli¹, Jonathan S. Oakhill¹², Michael F. Bailey, Sheena Wee, Mark Walter³, Bryce J. van Denderen, Laura A. Castelli^¶, Frosa Katsis, Lee A. Witters^||, David Stapleton, S. Lance Macaulay^¶, Belinda J. Michell⁴, and Bruce E. Kemp^¶5

From the St. Vincent's Institute, Fitzroy, Victoria 3065, Australia, Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia, ^||Endocrine-Metabolism Division, Departments of Medicine and Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3833, and ^¶CSIRO Molecular Health Technologies, Parkville, Victoria 3052, Australia

AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic subunit and two non-catalytic subunits, β and , each with multiple isoforms that form active 1:1:1 heterotrimers. Here we show that recombinant human AMPK 1β11 expressed in insect cells is monomeric and displays specific activity and AMP responsiveness similar to rat liver AMPK. The previously determined crystal structure of the core of mammalian β complex shows that β binds and . Here we show that a β1(186–270)1 complex can form in the absence of detectable subunit. Moreover, using alanine mutagenesis we show that β1 Thr-263 and Tyr-267 are required for β association but not β association.

Received for publication, October 5, 2007 , and in revised form, December 10, 2007.

^* This study was supported by grants from the Australian Research Council (to B. E. K.), National Health and Medical Research Council (to B. E. K.), National Heart Foundation (to B. E. K.), and National Institutes of Health Grant DK35712 (to L. A. W.). 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.

¹ Both authors contributed equally to this study.

³ Current address: Dept. of Biochemistry and Molecular Biology, Monash University, Clayton Victoria 3800.

⁵ Australian Research Council Federation Fellow.

² To whom correspondence may be addressed: St. Vincent's Institute, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia. Tel.: 61-3-92882480; Fax: 61-3-94162676; E-mail: joakhill{at}svi.edu.au. ⁴ To whom correspondence may be addressed: St. Vincent's Institute, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia. Tel.: 61-3-92882480; Fax: 61-3-94162676; E-mail: bmichell{at}svi.edu.au.

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