AMP-activated
protein kinase (AMPK) is a heterotrimeric complex composed of a catalytic αsubunit and regulatory β and γ subunits. Each subunit has at least two
different isoforms, which are encoded by distinct genes.
They differ slightly
in their structure and have differential expression patterns across tissues.
The α subunit exists as 2 isoforms (α1 and α2), contains the AMPK
serine/threonine kinase domain, and is phosphorylated on at least three
residues Phosphorylation of threonine 172 by upstream kinases is essential for
AMPK activity, and is often used as an indicator of the activation state of the
kinase. Read more>>>>>>>>>>
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