Multiple pathways for mitochondrial protein traffic
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Toshiya Endo
Abstract
Mitochondria are two-membrane bounded organelles consisting of 1000–2000 different proteins, most of which are synthesized in the cytosol and subsequently imported into mitochondria. The imported proteins are further sorted to one of the four compartments, the outer membrane, intermembrane space, inner membrane, and matrix, mostly following one of the five major pathways. Mitochondrial protein import and sorting are mediated by the translocator complexes in the membranes and chaperones in the aqueous compartments operating along the import pathways. Here, we summarize the expanding knowledge on the roles of translocators, chaperones, and related components in the multiple pathways for mitochondrial protein trafficking.
©2009 by Walter de Gruyter Berlin New York
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- On the fate of early endosomes
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- The peptide-loading complex – antigen translocation and MHC class I loading
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Articles in the same Issue
- Guest Editorial
- Highlight: The gatekeepers of life yield their secrets
- Highlight: Membrane Transport and Communication
- First structural insights into the TpsB/Omp85 superfamily
- Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
- Structural and functional aspects of the multidrug efflux pump AcrB
- From the Sec complex to the membrane insertase YidC
- Emerging roles of mitochondrial membrane dynamics in health and disease
- Mitochondrial tRNA import – the challenge to understand has just begun
- Multiple pathways for mitochondrial protein traffic
- Challenges to our current view on chloroplasts
- Molecular interactions within the plant TOC complex
- Protein transport across the peroxisomal membrane
- On the fate of early endosomes
- ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
- Protein targeting by the signal recognition particle
- The peptide-loading complex – antigen translocation and MHC class I loading
- Protein-lipid interactions: paparazzi hunting for snap-shots
- The nanodisc: a novel tool for membrane protein studies
- NMR and EPR studies of membrane transporters