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Trends in Cell & Molecular Biology   Volumes    Volume 12 
Abstract
A role for ataxia telangiectasia mutated in insulin-independent stimulation of glucose transport
Larry D. Spears, Allyson L. Renth, Michael R. McKuin, Anne R. Kennedy, Stanley Andrisse, Nell E. Briggs, Jonathan S. Fisher
Pages: 49 - 56
Number of pages: 8
Trends in Cell & Molecular Biology
Volume 12 

Copyright © 2017 Research Trends. All rights reserved

ABSTRACT
 
Literature reports suggest that ataxia telangiectasia mutated (ATM) can activate the AMP-activated protein kinase (AMPK), a protein that can stimulate glucose transport in skeletal muscle. We hypothesized that 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), an AMPK activator, would increase glucose transport in mouse extensor digitorum longus (EDL) muscles in an ATM-dependent manner. AICAR-stimulated glucose transport was prevented by the ATM inhibitor KU-55933 despite normal stimulation of AMPK phosphorylation. Consistent with this, AICAR caused AMPK phosphorylation but not an increase of glucose transport in ATM-deficient (ATM-/-) muscles. S231 of TBC1D1 matches the sequence motif of ATM substrates, and phosphorylation of this site is known to inhibit TBC1D1 and lead to increased glucose transport. Accordingly, we assessed TBC1D1 phosphorylation and found that AICAR-stimulated phosphorylation of TBC1D1 at S231 did not occur in ATM-/- muscles. However, activation of ATM without activation of AMPK was insufficient to increase TBC1D1 phosphorylation. The data suggest that ATM plays a role in AICAR-stimulated glucose transport downstream of AMPK.
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