Journal
EUROPEAN JOURNAL OF CELL BIOLOGY
Volume 89, Issue 2-3, Pages 212-215Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ejcb.2009.11.002
Keywords
Mim1; TOM complex assembly; Mitochondria; Structure-function relationship
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Funding
- Deutsche Forschungsgemeinschaft [446-A30]
- Carl Zeiss Stiftung
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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. (C) 2009 Elsevier GmbH. All rights reserved.
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