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. 2011 Jan 5;286(14):11929–11936. doi: 10.1074/jbc.M110.189779

FIGURE 2.

FIGURE 2.

AMPK-dependent phosphorylation of BKCa splice variants. Autoradiogram (32P) and Coomassie Blue-stained gel and autoradiogram demonstrating phosphorylation of the STREX (A) and ZERO (B) splice variants of BKCa by AMPK purified from rat liver extract in the presence and absence of 200 μm AMP. C, autoradiogram and Coomassie Blue-stained gel demonstrating phosphorylation of the ZERO and STREX variants by human AMPK (α2β2γ1; 10 units/ml), showing the greater degree of phosphorylation of the STREX variant. D, autoradiogram and Coomassie Blue-stained gel demonstrating phosphorylation of the STREX variant and the S657A STREX mutant by human AMPK (α2β2γ1; 10 units/ml), showing the lower degree of phosphorylation of the S657A mutant. Note that for observations analyzed on a fixed percentage acrylamide protein gel, STREX and ZERO protein migrated at 137 and 131 kDa, respectively. In contrast, when analyzed on a 4–12% BisTris precast gel (Invitrogen), the STREX and ZERO proteins migrated with a smaller apparent mass of 97 and 90 kDa, respectively.