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Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A.

Molecular cell | Apr 27, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10230394

Signaling pathways between cell surface receptors and the BCL-2 family of proteins regulate cell death. Survival factors induce the phosphorylation and inactivation of BAD, a proapoptotic member. Purification of BAD kinase(s) identified membrane-based cAMP-dependent protein kinase (PKA) as a BAD Ser-112 (S112) site-specific kinase. PKA-specific inhibitors blocked the IL-3-induced phosphorylation on S112 of endogenous BAD as well as mitochondria-based BAD S112 kinase activity. A blocking peptide that disrupts type II PKA holoenzyme association with A-kinase-anchoring proteins (AKAPs) also inhibited BAD phosphorylation and eliminated the BAD S112 kinase activity at mitochondria. Thus, the anchoring of PKA to mitochondria represents a focused subcellular kinase/substrate interaction that inactivates BAD at its target organelle in response to a survival factor.

Pubmed ID: 10230394 RIS Download

Mesh terms: Animals | Apoptosis | Carrier Proteins | Cyclic AMP-Dependent Protein Kinase Type II | Cyclic AMP-Dependent Protein Kinases | Enzyme Activation | Enzyme Inhibitors | Interleukin-3 | Mitochondria | Phosphorylation | Proto-Oncogene Proteins c-bcl-2 | Signal Transduction | Tumor Cells, Cultured | bcl-Associated Death Protein

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