Cooperation of translocase complexes in mitochondrial protein import
Stephan Kutik, Bernard Guiard, Helmut E. Meyer, Nils Wiedemann, Nikolaus Pfanner
Abstract
Stephan Kutik, Bernard Guiard, Helmut E. Meyer, Nils Wiedemann, Nikolaus Pfanner
Abstract
Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. These translocase complexes do not act as independent units but cooperate with each other and further membrane complexes in a dynamic manner. We propose that a regulated coupling of translocases is important for the coordination of preprotein translocation and efficient sorting to intramitochondrial compartments.
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Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. These translocase complexes do not act as independent units but cooperate with each other and further membrane complexes in a dynamic manner. We propose that a regulated coupling of translocases is important for the coordination of preprotein translocation and efficient sorting to intramitochondrial compartments.
Key concepts: Intermembrane space, Translocase, Translocase of the outer membrane, Translocase of the inner membrane, Biology, Protein targeting, Mitochondrial carrier, ATP–ADP translocase