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 +5 more
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TLDR
Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin, resulting in unopposed fusion.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.read more
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Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure.
TL;DR: Placement of bioenergetic adaptation and quality control as competing tasks of mitochondrial dynamics might provide a new mechanism, linking excess nutrient environment to progressive mitochondrial dysfunction, common to age-related diseases.
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Fusion and Fission: Interlinked Processes Critical for Mitochondrial Health
TL;DR: By enabling content mixing between mitochondria, fusion and fission serve to maintain a homogeneous and healthy mitochondrial population and lead to improvements in human health.
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Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
TL;DR: Mitochondrial fission requires recruitment of the GTPase Drp1 to mitochondria, but the molecules that mediate this recruitment have been disputed.
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Mitochondrial dynamics: overview of molecular mechanisms
TL;DR: An overview of the molecular mechanisms that govern mitochondrial fission and fusion in mammals is described and several members of the machinery can undergo post-translational modifications modulating these processes.
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Structure and function of ER membrane contact sites with other organelles.
TL;DR: The structure and functions of MCSs are described, primarily focusing on contacts of the ER with mitochondria and endosomes, as well as engaging in organelle biogenesis and dynamics.
References
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Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
TL;DR: It is shown that mutations in the human dynamin-related protein Drp1 cause mitochondria to form perinuclear clusters that consist of highly interconnected mitochondrial tubules, which indicates that the balance between mitochondrial division and fusion is shifted toward fusion.
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Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells.
Hidenori Otera,Chunxin Wang,Megan M. Cleland,Kiyoko Setoguchi,Sadaki Yokota,Richard J. Youle,Katsuyoshi Mihara +6 more
TL;DR: Localization of the dynamin-related GTPase Drp1 to mitochondria relies on the mitochondrial fission factor Mff.
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Mitochondrial Dynamics in Mammalian Health and Disease
TL;DR: Findings in the field of mitochondrial dynamics in mammalian cells and their implication in human pathologies have established mitochondrial dynamics as a consolidated area in cellular physiology.