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Mitochondrial Protein Import Under Kinase Surveillance

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Journal Microb Cell
Specialty Microbiology
Date 2017 Mar 31
PMID 28357222
Citations 6
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Abstract

Despite the simplicity of the yeast its basic cellular machinery tremendously mirrors that of higher eukaryotic counterparts. Thus, this unicellular organism turned out to be an invaluable model system to study the countless mechanisms that govern life of the cell. Recently, it has also enabled the deciphering of signalling pathways that control flux of mitochondrial proteins to the organelle according to metabolic requirements. For decades mitochondria were considered autonomous organelles that are only partially incorporated into cellular signalling networks. Consequently, only little has been known about the role of reversible phosphorylation as a meaningful mechanism that orchestrates mitochondrial biology accordingly to cellular needs. Therefore, research in this direction has been vastly neglected. However, findings over the past few years have changed this view and new exciting fields in mitochondrial biology have emerged. Here, we summarize recent discoveries in the yeast model system that point towards a vital role of reversible phosphorylation in regulation of mitochondrial protein import.

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References
1.
Pagliarini D, Calvo S, Chang B, Sheth S, Vafai S, Ong S . A mitochondrial protein compendium elucidates complex I disease biology. Cell. 2008; 134(1):112-23. PMC: 2778844. DOI: 10.1016/j.cell.2008.06.016. View

2.
Cohen P . Protein kinases--the major drug targets of the twenty-first century?. Nat Rev Drug Discov. 2002; 1(4):309-15. DOI: 10.1038/nrd773. View

3.
Vancura A, Sessler A, Leichus B, Kuret J . A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast. J Biol Chem. 1994; 269(30):19271-8. View

4.
Rao S, Gerbeth C, Harbauer A, Mikropoulou D, Meisinger C, Schmidt O . Signaling at the gate: phosphorylation of the mitochondrial protein import machinery. Cell Cycle. 2011; 10(13):2083-90. DOI: 10.4161/cc.10.13.16054. View

5.
Stojanovski D, Muller J, Milenkovic D, Guiard B, Pfanner N, Chacinska A . The MIA system for protein import into the mitochondrial intermembrane space. Biochim Biophys Acta. 2007; 1783(4):610-7. DOI: 10.1016/j.bbamcr.2007.10.004. View