Detection of Protein Kinase A and C Target Proteins in Rat Brain Mitochondria

Abstract Phosphorylation of some membrane-bound proteins in the mitochondria of rat liver and brain is regulated by $ Ca^{2+} $ and cAMP acting as secondary messengers. These proteins are the main myelin components: 46 kDa 2′,3′-cyclic-nucleotide 3′-phosphodiesterase (CNP) and two isoforms of the my...
Ausführliche Beschreibung

Abstract Phosphorylation of some membrane-bound proteins in the mitochondria of rat liver and brain is regulated by $ Ca^{2+} $ and cAMP acting as secondary messengers. These proteins are the main myelin components: 46 kDa 2′,3′-cyclic-nucleotide 3′-phosphodiesterase (CNP) and two isoforms of the myelin basic protein (MBP) with molecular weights of 17 and 21.5 kDa, which we have identified previously and found outside myelin in rat brain mitochondria. The phosphorylation level of CNP and both MBP isoforms increases when the mitochondrial permeability transition pore (mPTP) is opened. It is known that protein kinases A and C in heart mitochondria are directly bound to mPTP regulator proteins and are able to modulate the pore function. It is shown in this study that the inhibitors of protein kinases A (H-89) and C (staurosporin, Go 6976, and GF 109203 X) decrease the phosphorylation level of CNP and two MBP isoforms allowing us to assume that they are the targets of the signaling protein kinases A and C. Ausführliche Beschreibung