MiD49 and MiD51, new components of the mitochondrial fission machinery

Catherine S. Palmer; Laura D. Osellame; David Laine; Olga S. Koutsopoulos; Ann E Frazier; Michael T. Ryan

doi:10.1038/embor.2011.54

MiD49 and MiD51, new components of the mitochondrial fission machinery

Catherine S. Palmer, Laura D. Osellame, David Laine, Olga S. Koutsopoulos, Ann E Frazier, Michael T. Ryan

Research output: Contribution to journal › Article › Research › peer-review

459 Citations (Scopus)

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 mitochondria.

Original language	English
Pages (from-to)	565-573
Number of pages	9
Journal	EMBO Reports
Volume	12
Issue number	6
DOIs	https://doi.org/10.1038/embor.2011.54
Publication status	Published - Jun 2011
Externally published	Yes

Keywords

Drp1
fission
fusion
mitochondria
morphology

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10.1038/embor.2011.54

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title = "MiD49 and MiD51, new components of the mitochondrial fission machinery",

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 mitochondria.",

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AU - Palmer, Catherine S.

AU - Osellame, Laura D.

AU - Laine, David

AU - Koutsopoulos, Olga S.

AU - Frazier, Ann E

AU - Ryan, Michael T.

PY - 2011/6

Y1 - 2011/6

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AB - 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 mitochondria.

KW - Drp1

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KW - fusion

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KW - morphology

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MiD49 and MiD51, new components of the mitochondrial fission machinery

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Keywords

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