期刊
MOLECULAR BIOLOGY OF THE CELL
卷 23, 期 9, 页码 1618-1627出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-11-0933
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资金
- Deutsche Forschungsgemeinschaft
- Excellence Initiative of the German Federal Government (GSC-4 Spemann Graduate School) [EXC 294 BIOSS]
- Excellence Initiative of the German State Government (GSC-4 Spemann Graduate School) [EXC 294 BIOSS]
- Trinationales Graduiertenkolleg [GRK 1478]
- Sonderforschungsbereich [746]
- Bundesministerium fur Bildung und Forschung (Dynamo)
- Landesforschungspreis Baden-Wurttemberg
- Gottfried Wilhelm Leibniz Program
The preprotein translocase of the outer mitochondrial membrane (TOM) functions as the main entry gate for the import of nuclear-encoded proteins into mitochondria. The major subunits of the TOM complex are the three receptors Tom20, Tom22, and Tom70 and the central channel-forming protein Tom40. Cytosolic kinases have been shown to regulate the biogenesis and activity of the Tom receptors. Casein kinase 2 stimulates the biogenesis of Tom22 and Tom20, whereas protein kinase A (PKA) impairs the receptor function of Tom70. Here we report that PKA exerts an inhibitory effect on the biogenesis of the beta-barrel protein Tom40. Tom40 is synthesized as precursor on cytosolic ribosomes and subsequently imported into mitochondria. We show that PKA phosphorylates the precursor of Tom40. The phosphorylated Tom40 precursor is impaired in import into mitochondria, whereas the non-phosphorylated precursor is efficiently imported. We conclude that PKA plays a dual role in the regulation of the TOM complex. Phosphorylation by PKA not only impairs the receptor activity of Tom70, but it also inhibits the biogenesis of the channel protein Tom40.
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