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Am J Physiol Cell Physiol (September 24, 2003). doi:10.1152/ajpcell.00319.2003
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Submitted on July 25, 2003
Accepted on September 17, 2003

Cloning and Characterization of Mouse 5'-AMP Activated Protein Kinase {gamma}3 Subunit

Haiyan Yu1, Nobuharu Fujii1, Mike F Hirshman1, Jason M Pomerleau1, and Laurie J Goodyear1*

1 Reasearch Division, Joslin Diabetes Center, Harvard Medical School, Boston, MA, USA

* To whom correspondence should be addressed. E-mail: laurie.goodyear{at}joslin.harvard.edu.

Naturally occurring mutations in the regulatory {gamma} subunit of 5[[rad]]-AMP activated protein kinase (AMPK) can result in pronounced pathological changes that may stem from increases in muscle glycogen levels, making it critical to understand the role(s) of the {gamma} subunit in AMPK function. In this study we cloned the mouse AMPK{gamma}3 subunit and revealed that there are two transcription start sites, which result in a long form, {gamma}3L (AF525500) and a short form, {gamma}3S (AF525501). AMPK{gamma}3L is the predominant form in mouse and is specifically expressed in mouse skeletal muscle at the protein level. In skeletal muscle, AMPK{gamma}3 shows higher levels of expression in fast-twitch white glycolytic muscle (type IIb) compared to fast-twitch red oxidative glycolytic muscle (type IIa), whereas {gamma}3 is undetectable in soleus muscle, a slow-twitch oxidative muscle with predominantly type I fibers. AMPK{gamma}3 can co-immunoprecipititate with both {alpha} and {beta} AMPK subunits. Overexpression of {gamma}3S and {gamma}3L in mouse tibialis anterior muscle in vivo has no effect on {alpha}1 and {alpha}2 subunit expression and does not alter AMPK{alpha}2 catalytic activity. However, {gamma}3S and {gamma}3L overexpression significantly increases AMPK{alpha}1 phosphorylation and activity by approximately 50%. The increase in AMPK{alpha}1 activity is not associated with alterations in glycogen accumulation or glycogen synthase expression. In conclusion, the {gamma}3 subunit of AMPK is highly expressed in fast-twitch glycolytic skeletal muscle, and wild type {gamma}3 functions in the regulation of {alpha}1 catalytic activity, but it is not associated with changes in muscle glycogen concentrations.




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