Protein Phosphorylation in Rat Liver Mitochondria

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1990 Sep 3

PMID 2247049

Citations 2

Authors

S Ferrari

V Moret

N SILIPRANDI

Affiliations

Soon will be listed here.

Abstract

Incubation of rat liver mitochondria in the presence of either [32P] Pi or [y32-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 different 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.

Citing Articles

Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism.

Phillips D, Aponte A, French S, Chess D, Balaban R Biochemistry. 2009; 48(30):7140-9.

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Structure, function and regulation of the tricarboxylate transport protein from rat liver mitochondria.

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