Importing Mitochondrial Proteins: Machineries and Mechanisms
By A. Chacińska, C. Koehler, Dusanka Milenkovic, T. Lithgow, N. Pfanner. Cell, 2009
1,419 citations recorded by the source corpus.
Most mitochondrial proteins are synthesized on cytosolic ribosomes and must be imported across one or both mitochondrial membranes. There is an amazingly versatile set of machineries and mechanisms, and at least four different pathways, for the importing and sorting of mitochondrial precursor proteins. The translocases that catalyze these processes are highly dynamic machines driven by the membrane potential, ATP, or redox reactions, and they cooperate with molecular chaperones and assembly complexes to direct mitochondrial proteins to their correct destinations. Here, we discuss recent insights into the importing and sorting of mitochondrial proteins and their contributions to mitochondrial biogenesis.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7882f2ca48b4af4f43a0e461697edbdaae62aea6
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Citations in the corpus
- Mitochondrial protein import: from proteomics to functional mechanisms (2010, background): “The common entry gate for most precursors is formed by the translocase of the outer membrane (TOM) comple”
- MitoFates: Improved Prediction of Mitochondrial Targeting Sequences and Their Cleavage Sites (2015, background): “Given that Tom20 and Tom22 in the TOM complex most likely recognize an amphiphilic helical local structure consisting of hydrophobic and positively charged faces (6, 12, 13), we conjectured that a score that favors positive charges on the polar face might better characterize presequences.”
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