A fuzzy mitochondrial fusion apparatus comes into focus (Q35141756)

6 August 2017

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title

A fuzzy mitochondrial fusion apparatus comes into focus (English)

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6 August 2017

main subject

Fuzzy onions Dmel_CG4568

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GOA release 2020-03-11

author name string

Amy D Mozdy

series ordinal

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6 August 2017

Janet M Shaw

series ordinal

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6 August 2017

publication date

1 June 2003

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Nature Reviews Molecular Cell Biology

6 August 2017

published in

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6 August 2017

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6 August 2017

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6 August 2017

page(s)

468-478

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Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria

6 August 2017

cites work

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Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA

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Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase.

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Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p

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Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae

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UGO1 encodes an outer membrane protein required for mitochondrial fusion

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Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane

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The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion

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Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape

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C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane

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Division of mitochondria requires a novel DMN1-interacting protein, Net2p

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Gag3p, an outer membrane protein required for fission of mitochondrial tubules

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Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p

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Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division

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The many shapes of mitochondrial membranes

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Mitochondrial division: New partners in membrane pinching

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Merging mitochondria matters: cellular role and molecular machinery of mitochondrial fusion

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OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28

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Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy

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Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis

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Mitochondrial filaments and clusters as intracellular power-transmitting cables

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SNARE-mediated membrane fusion

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Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development

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Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin

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Dynamin and its role in membrane fission

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The GTPase effector domain sequence of the Dnm1p GTPase regulates self-assembly and controls a rate-limiting step in mitochondrial fission

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Primary structure of a dynamin-related mouse mitochondrial GTPase and its distribution in brain, subcellular localization, and effect on mitochondrial morphology

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CYTOKINESIS AND BUILDING OF THE CELL PLATE IN PLANTS.

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Highly conserved charge-pair networks in the mitochondrial carrier family

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Mechanisms of membrane fusion

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Structure of influenza haemagglutinin at the pH of membrane fusion

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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

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Influenza hemagglutinin is spring-loaded by a metastable native conformation

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Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion.

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Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

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Identifiers

DOI

10.1038/NRM1125

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6 August 2017

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