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MUSCLE CELL BIOLOGY AND CELL MOTILITY

Cloning and characterization of mouse 5'-AMP-activated protein kinase 3 subunit

Research Division, Joslin Diabetes Center, and Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02215

Submitted 25 July 2003 ; accepted in final form 17 September 2003

Naturally occurring mutations in the regulatory -subunit of 5'-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 -subunit in AMPK function. In this study we cloned the mouse AMPK3 subunit and revealed that there are two transcription start sites, which result in a long form, 3L (AF525500) and a short form, 3S (AF525501). AMPK3L is the predominant form in mouse and is specifically expressed in mouse skeletal muscle at the protein level. In skeletal muscle, AMPK3 shows higher levels of expression in fast-twitch white glycolytic muscle (type IIb) compared with fast-twitch red oxidative glycolytic muscle (type IIa), whereas 3 is undetectable in soleus muscle, a slow-twitch oxidative muscle with predominantly type I fibers. AMPK3 can coimmunoprecipititate with both and AMPK subunits. Overexpression of 3S and 3L in mouse tibialis anterior muscle in vivo has no effect on 1 and 2 subunit expression and does not alter AMPK2 catalytic activity. However, 3S and 3L overexpression significantly increases AMPK1 phosphorylation and activity by 50%. The increase in AMPK1 activity is not associated with alterations in glycogen accumulation or glycogen synthase expression. In conclusion, the 3 subunit of AMPK is highly expressed in fast-twitch glycolytic skeletal muscle, and wild-type 3 functions in the regulation of 1 catalytic activity, but it is not associated with changes in muscle glycogen concentrations.

adenosine 5'-monophosphate-activated protein kinase; AMPK3 short form; AMPK3 long form; cystathionine -synthase domain

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