期刊
JOURNAL OF CELL BIOLOGY
卷 185, 期 6, 页码 1047-1063出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200811099
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资金
- Deutsche Forschungsgemeinschaft Sonderforschungsbereich 594 project B8
- Cluster of Excellence Macromolecular Complexes at the Goethe University Frankfurt Deutsche Forschungsgemeinschaft [EXC 115]
- Center for Integrated Protein Science Munchen, the Fondation pour la Recherche Medicale
- Federation of European Biochemical Societies
Crista junctions (CJs) are important for mitochondrial organization and function, but the molecular basis of their formation and architecture is obscure. We have identified and characterized a mitochondrial membrane protein in yeast, Fcj1 (formation of CJ protein 1), which is specifically enriched in CJs. Cells lacking Fcj1 lack CJs, exhibit concentric stacks of inner membrane in the mitochondrial matrix, and show increased levels of F1FO-ATP synthase (F1FO) super-complexes. Overexpression of Fcj1 leads to increased CJ formation, branching of cristae, enlargement of CJ diameter, and reduced levels of F1FO supercomplexes. Impairment of F1FO oligomer formation by deletion of its subunits e/g (Su e/g) causes CJ diameter enlargement and reduction of cristae tip numbers and promotes cristae branching. Fcj1 and Su e/g genetically interact. We propose a model in which the antagonism between Fcj1 and Su e/g locally modulates the F1FO oligomeric state, thereby controlling membrane curvature of cristae to generate CJs and cristae tips.
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