[HTML][HTML] Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP
RL Hurley, LK Barré, SD Wood, KA Anderson… - Journal of Biological …, 2006 - ASBMB
The AMP-activated protein kinase (AMPK) and cAMP signaling systems are both key
regulators of cellular metabolism. In this study, we show that AMPK activity is attenuated in
response to cAMP-elevating agents through modulation of at least two of its α subunit
phosphorylation sites, viz. α-Thr 172 and α1-Ser 485/α2-Ser 491, in the clonal β-cell line INS-
1 as well as in mouse embryonic fibroblasts and COS cells. Forskolin,
isobutylmethylxanthine, and the glucose-dependent insulinotropic peptide inhibited AMPK …
regulators of cellular metabolism. In this study, we show that AMPK activity is attenuated in
response to cAMP-elevating agents through modulation of at least two of its α subunit
phosphorylation sites, viz. α-Thr 172 and α1-Ser 485/α2-Ser 491, in the clonal β-cell line INS-
1 as well as in mouse embryonic fibroblasts and COS cells. Forskolin,
isobutylmethylxanthine, and the glucose-dependent insulinotropic peptide inhibited AMPK …