Journal article
MiD49 and MiD51, new components of the mitochondrial fission machinery
CS Palmer, LD Osellame, D Laine, OS Koutsopoulos, AE Frazier, MT Ryan
EMBO Reports | NATURE PUBLISHING GROUP | Published : 2011
Abstract
Mitochondria form intricate networks through fission and fusion events. Here, we identify mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) anchored in the mitochondrial outer membrane. MiD49/51 form foci and rings around mitochondria similar to the fission mediator dynamin-related protein 1 (Drp1). MiD49/51 directly recruit Drp1 to the mitochondrial surface, whereas their knockdown reduces Drp1 association, leading to unopposed fusion. Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin. Thus, MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondri..
View full abstractGrants
Funding Acknowledgements
We thank D. Chudakov, J. Shaw, L. Scorrano, A. van der Bliek, R. Youle, E. Hanssen, Q. Zhao and X. Wang for various constructs, reagents and assistance. This work was supported by grants from the National Health and Medical Research Council, Australian Research Council, the William Buckland Foundation and the Human Frontier Science Program Organization.