Fidelity of organellar protein targeting |
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| Affiliation: | 1. Osnabrück University, Department of Biology/Chemistry, Molecular Membrane Biology Group, Barbarastraße 13, 49076 Osnabrück, Germany;2. Osnabrück University, Center of Cellular Nanoanalytics Osnabrück (CellNanOs), Barbarastrasse 11, 49076 Osnabrück, Germany;1. Department of Medical Genetics, University of British Columbia, Vancouver, BC VH6 3N1, Canada;2. Centre for Molecular Medicine and Therapeutics, British Columbia Children''s Hospital Research Institute, University of British Columbia, Vancouver, BC V5Z 4H4, Canada;1. Department of Molecular Medicine, Institute of Basic Medical Sciences and Centre for Cancer Cell Reprogramming, Institute of Clinical Medicine, University of Oslo, 0372 Oslo, Norway;2. Department of Molecular Cell Biology, The Norwegian Radium Hospital Montebello, 0379, Oslo, Norway;3. Membrane Biochemistry and Transport, Institut Pasteur, UMR3691 CNRS, 75015, Paris, France;1. IEO, Istituto Europeo di Oncologia IRCCS, Via Ripamonti 435, 20141, Milan, Italy;2. Università degli Studi di Milano, Dipartimento di Oncologia ed Emato-oncologia, Via Santa Sofia 9/1, 20122, Milan, Italy;3. University of Texas, Department of Biomedical Engineering, 107 W. Dean Keeton St., C0800, Austin, TX, USA |
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| Abstract: | The majority of cellular proteins are targeted to organelles. Cytosolic ribosomes produce these proteins as precursors with cleavable or non-cleavable targeting sequences that direct them to receptor proteins on the organelle surface. Multiple targeting factors ensure cellular sorting of the precursor proteins. In co-translational protein import, the ribosome-nascent chain complex is transported to the organellar protein translocase to couple protein synthesis and protein import. In post-translational mode, targeting factors like molecular chaperones guide the precursor proteins from ribosomes to the cell organelle. Defects in protein targeting and import cause mistargeting of proteins to different cellular compartments and challenge the balance of cellular proteostasis. Specific dislocases and degradation machineries remove such mislocalized proteins from the membrane to allow retargeting or their proteasomal turnover. In this review, we discuss targeting and quality control factors that ensure fidelity of protein targeting to mitochondria. |
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