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Mim1 在线粒体生物发生中的神秘作用。

The enigmatic role of Mim1 in mitochondrial biogenesis.

机构信息

Interfaculty Institute for Biochemistry, University of Tübingen, Hoppe-Seyler-Strasse 4, 72076 Tübingen, Germany.

出版信息

Eur J Cell Biol. 2010 Feb-Mar;89(2-3):212-5. doi: 10.1016/j.ejcb.2009.11.002. Epub 2009 Nov 26.

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.

摘要

外膜线粒体转位酶(TOM 复合物)是一种多亚基复合物,作为新合成的蛋白质进入细胞器的通用进入位点。该复合物的组装是一个多步骤的过程,需要几种蛋白质的协调作用。在此过程中,扮演核心但定义不明确角色的是 Mim1,一种线粒体外膜蛋白。MIM1 的缺失导致 TOM 复合物亚基的生物发生严重缺陷,并改变线粒体形态。该蛋白由一个 N 端胞质结构域、一个中央跨膜片段和一个面向膜间空间的 C 端结构域组成。在这篇综述中,我们总结了目前对 Mim1 的结构-功能关系的认识,并讨论了其分子功能的一些可能性。

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