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Dynamic subcompartmentalization of the mitochondrial inner membrane

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Item Type:Article
Title:Dynamic subcompartmentalization of the mitochondrial inner membrane
Creators Name:Vogel, F. and Bornhoevd, C. and Neupert, W. and Reichert, A.S.
Abstract:The inner membrane of mitochondria is organized in two morphologically distinct domains, the inner boundary membrane (IBM) and the cristae membrane (CM), which are connected by narrow, tubular cristae junctions. The protein composition of these domains, their dynamics, and their biogenesis and maintenance are poorly understood at the molecular level. We have used quantitative immunoelectron microscopy to determine the distribution of a collection of representative proteins in yeast mitochondria belonging to seven major processes: oxidative phosphorylation, protein translocation, metabolite exchange, mitochondrial morphology, protein translation, iron-sulfur biogenesis, and protein degradation. We show that proteins are distributed in an uneven, yet not exclusive, manner between IBM and CM. The individual distributions reflect the physiological functions of proteins. Moreover, proteins can redistribute between the domains upon changes of the physiological state of the cell. Impairing assembly of complex III affects the distribution of partially assembled subunits. We propose a model for the generation of this dynamic subcompartmentalization of the mitochondrial inner membrane.
Keywords:Cell Compartmentation, Immunoenzyme Techniques, Intracellular Membranes, Mitochondria, Mitochondrial Membranes, Mitochondrial Proteins, Oxidative Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Source:Journal of Cell Biology
Publisher:Rockefeller University Press
Page Range:237-247
Date:23 October 2006
Additional Information:Copyright (c) 2006 by Rockefeller University Press
Official Publication:https://doi.org/10.1083/jcb.200605138
PubMed:View item in PubMed

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