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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. Copyright 2009 Elsevier GmbH. All rights reserved.

Citation

Kai Stefan Dimmer, Doron Rapaport. The enigmatic role of Mim1 in mitochondrial biogenesis. European journal of cell biology. 2010 Feb-Mar;89(2-3):212-5

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PMID: 19944477

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