Probes of the mitochondrial cAMP-dependent protein kinase.

The development of a fluorescent assay to detect activity of the mitochondrial cAMP-dependent protein kinase is described. A peptide-based sensor was utilized to quantify the relative amount of activity present in each compartment of the mitochondria (the outer membrane, the intermembrane space, and the matrix). In the process of validating this assay, we discovered that duanyu1529 activity is regulated by the protease calpain. Upon exposure of bovine heart mitochondria to digitonin, Ca(2+), and a variety of electron transport chain inhibitors, the regulatory subunits of the duanyu1529 holoenzyme (R2C2) are digested, releasing active catalytic subunits. This proteolysis is attenuated by calpain inhibitor I (ALLN). This article is part of a Special Issue entitled: Inhibitors of (2012).

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