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The inner membrane protein Mdm33 controls mitochondrial morphology in yeast

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Official URL:https://doi.org/10.1083/jcb.200211113
PubMed:View item in PubMed
Creators Name:Messerschmitt, M. and Jakobs, S. and Vogel, F. and Fritz, S. and Dimmer, K.S. and Neupert, W. and Westermann, B.
Journal Title:Journal of Cell Biology
Journal Abbreviation:J Cell Biol
Volume:160
Number:4
Page Range:553-564
Date:18 February 2003
Keywords:Membrane Fission, Mitochondria, Mitochondrial Dynamics, Organelle Morphology, Saccharomyces Cerevisiae
Abstract:Mitochondrial distribution and morphology depend on MDM33, a Saccharomyces cerevisiae gene encoding a novel protein of the mitochondrial inner membrane. Cells lacking Mdm33 contain ring-shaped, mostly interconnected mitochondria, which are able to form large hollow spheres. On the ultrastructural level, these aberrant organelles display extremely elongated stretches of outer and inner membranes enclosing a very narrow matrix space. Dilated parts of Delta mdm33 mitochondria contain well-developed cristae. Overexpression of Mdm33 leads to growth arrest, aggregation of mitochondria, and generation of aberrant inner membrane structures, including septa, inner membrane fragments, and loss of inner membrane cristae. The MDM33 gene is required for the formation of net-like mitochondria in mutants lacking components of the outer membrane fission machinery, and mitochondrial fusion is required for the formation of extended ring-like mitochondria in cells lacking the MDM33 gene. The Mdm33 protein assembles into an oligomeric complex in the inner membrane where it performs homotypic protein-protein interactions. Our results indicate that Mdm33 plays a distinct role in the mitochondrial inner membrane to control mitochondrial morphology. We propose that Mdm33 is involved in fission of the mitochondrial inner membrane.
ISSN:0021-9525
Publisher:Rockefeller University Press (U.S.A.)
Additional Information:Copyright (c) 2003 by The Rockefeller University Press
Item Type:Article

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