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From inventory to functional mechanisms
Author(s) -
Gerbeth Carolin,
Mikropoulou Despina,
Meisinger Chris
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12445
Subject(s) - phosphorylation , cytosol , organelle , microbiology and biotechnology , mitochondrion , saccharomyces cerevisiae , biology , mitochondrial matrix , phosphatase , protein phosphorylation , biochemistry , kinase , protein kinase a , enzyme , yeast
For decades, the pyruvate dehydrogenase complex in the mitochondrial matrix was considered as a rare example of how protein kinases and phosphatases can regulate important functions within this organelle. During the last decade, several proteomic studies revealed that a large fraction of mitochondrial proteins are indeed phosphorylated. A surprisingly high number of phosphorylation sites was found at the preprotein import machinery, TOM , in the outer membrane that provides the central protein import gate for most mitochondrial precursors synthesized in the cytosol. This review describes current knowledge of the mitochondrial phosphoproteome and introduces the first regulatory mechanisms of protein import dynamics by reversible phosphorylation, which have been uncovered mainly in the model organism Saccharomyces cerevisiae .