The enigmatic role of Mim1 in mitochondrial biogenesis

European Journal of Cell Biology
Kai Stefan Dimmer, Doron Rapaport

Abstract

The translocase of the outer mitochondrial membrane (TOM complex) is a multi-subunit complex that serves as the general entry site for newly synthesized proteins into the organelle. The assembly of this complex is a multi-step process that requires the coordinated action of several proteins. A central, but rather undefined role in this process is played by Mim1, a mitochondrial outer membrane protein. The deletion of MIM1 leads to severe defects in the biogenesis of TOM complex subunits and to altered mitochondrial morphology. The protein is built from an N-terminal cytosolic domain, a central transmembrane segment, and a C-terminal domain facing the intermembrane space. In this review we summarize our current knowledge on the structure-function relationship of Mim1 and discuss some possibilities for its molecular function.

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Citations

Aug 10, 2011·The Journal of Cell Biology·Drazen PapicDoron Rapaport
Sep 6, 2011·Biochimica Et Biophysica Acta·Kai Stefan Dimmer, Doron Rapaport
Jul 21, 2016·Proceedings of the National Academy of Sciences of the United States of America·Sandro KäserAndré Schneider
Dec 16, 2016·Traffic·Anke Harsman, André Schneider
May 20, 2015·Biological Chemistry·Lars EllenriederThomas Becker
Mar 7, 2020·Biological Chemistry·Maria Clara Avendaño-MonsalveSoledad Funes
Mar 7, 2020·Biological Chemistry·André Schneider
Apr 3, 2012·Journal of Cell Science·Kai S DimmerDoron Rapaport

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