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What does T172A stand for?

T172A stands for Thr(172) to an alanine residue

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We have used site-directed mutagenesis to study the role of phosphorylation of Thr(172) on AMPK activity. Mutation of Thr(172) to an aspartic acid residue (T172D) in either alpha1 or alpha2 resulted in a kinase complex with approx. 50% the activity of the corresponding wild-type complex. The activity of wild-type AMPK decreased by greater than 90% following treatment with protein phosphatases, whereas the activity of the T172D mutant complex fell by only 10-15%. Mutation of Thr(172) to an alanine residue.
We have used site-directed mutagenesis to study the role of phosphorylation of Thr(172) on AMPK activity. Mutation of Thr(172) to an aspartic acid residue (T172D) in either alpha1 or alpha2 resulted in a kinase complex with approx. 50% the activity of the corresponding wild-type complex. The activity of wild-type AMPK decreased by greater than 90% following treatment with protein phosphatases, whereas the activity of the T172D mutant complex fell by only 10-15%. Mutation of Thr(172) to an alanine residue.
To elucidate the molecular mechanism underlying PKA-mediated inhibition of AMPK activation by LKB1, we generated a non-phosphorylatable mutant of AMPKa1 in which Ser-173 was mutated to an alanine residue. The AMPKa1(S173A) mutant protein proved to be resistant to Thr-172 phosphorylation by LKB1, but was still phosphorylated at Ser-485 and Ser-497 by PKA (Figure 4A). One possible explanation of a failure of LKB1 to phosphorylate Thr-172 in AMPKa1 in the context of a Ser-173 to alanine mutation may relate to the fact that these two sites are located within the recognition sequence of LKB1.