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Published online November 12, 2007
doi:10.1083/jcb.200708199
The Journal of Cell Biology, Vol. 179, No. 4, 585-591
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Kutik et al.
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Cooperation of translocase complexes in mitochondrial protein import



Stephan Kutik1,2, Bernard Guiard3, Helmut E. Meyer4, Nils Wiedemann1, and Nikolaus Pfanner1

1 Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, and 2 Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany
3 Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, F-91190 Gif-sur-Yvette, France
4 Medizinisches Proteom-Center, Ruhr-Universität Bochum, 44780 Bochum, Germany

Correspondence to Nikolaus Pfanner: nikolaus.pfanner{at}biochemie.uni-freiburg.de

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.

Abbreviations used in this paper: Hsp, heat-shock protein; MDM, mitochondrial distribution and morphology; mtHsp70, mitochondrial Hsp70; PAM, presequence translocase-associated motor; SAM, sorting and assembly machinery; TOM, translocase of outer mitochondrial membrane.


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