Protein phosphorylation in rat liver mitochondria |
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Authors: | Stefano Ferrari Vittorio Moret Noris Siliprandi |
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Affiliation: | (1) Department of Biological Chemistry, University of Padova, Via Trieste 75, 35121 Padova;(2) CNR Unit for the Study of Mitochondrial Physiology, Padova, Italy;(3) Dipartimento di Chimica Biologica, Via Trieste, 75, 35121 Padova, Italy |
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Abstract: | Summary Incubation of rat liver mitochondria in the presence of either [32P] Pi or 32y-P] ATP resulted in a phosphorylation of four proteins with Mr 50, 47, 44 and 36 kDa, respectively. The endogenous phosphorylation of these proteins in the presence of [32P] Pi was markedly influenced by the osmolarity of the incubation medium and differentially affected by various effectors of mitochondrial functions, such as Ca2+, oligomycin, FCCP, arsenite and dichloroacetate. In particular, the 36 kDa protein, unlike the other proteins, appears to be phosphorylated also by direct incorporation of [32P], independently of respiratory chain-linked ATP synthesis. The four proteins, located in the mitoplasts, seem to be phosphorylated by diiferent protein kinases, as suggested by the observation that the endogenous phosphorylation of 36 kDa protein resulted selectively increased by addition of exogenous protein kinases, such as casein kinases S and TS. A tentative identification of these phosphorylatable protein is discussed. |
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Keywords: | mitochondrial protein phosphorylation casein kinases |
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