Aim24 and MICOS modulate respiratory function, tafazzin-related cardiolipin modification and mitochondrial architecture

eLife

Ann-Katrin Unger¹  Stefan Geimer¹  Benedikt Westermann¹  Fulvio Reggiori²  Cagakan Özbalci³  Britta Brügger³  Toshiaki Izawa⁴  Dirk M Walther⁴  Matthias Mann⁴  Walter Neupert⁴  Max Emanuel Harner⁴ 

[1] Cell Biology and Electron Microscopy, University of Bayreuth, Bayreuth, Germany;Department of Cell Biology, University Medical Centre Utrecht, Utrecht, Netherlands;Heidelberg University Biochemistry Centre, Heidelberg, Germany;Max Planck Institute of Biochemistry, Martinsried, Munich, Germany;

关键词: mitochondria;    contact sites;    MICOS complex;    cardiolipin;    aim24;    mitofilin;   

DOI  :  10.7554/eLife.01684

来源: DOAJ

【 摘 要 】

Structure and function of mitochondria are intimately linked. In a search for components that participate in building the elaborate architecture of this complex organelle we have identified Aim24, an inner membrane protein. Aim24 interacts with the MICOS complex that is required for the formation of crista junctions and contact sites between inner and outer membranes. Aim24 is necessary for the integrity of the MICOS complex, for normal respiratory growth and mitochondrial ultrastructure. Modification of MICOS subunits Mic12 or Mic26 by His-tags in the absence of Aim24 leads to complete loss of cristae and respiratory complexes. In addition, the level of tafazzin, a cardiolipin transacylase, is drastically reduced and the composition of cardiolipin is modified like in mutants lacking tafazzin. In conclusion, Aim24 by interacting with the MICOS complex plays a key role in mitochondrial architecture, composition and function.

【 授权许可】

Unknown