Mitofusin 2 tethers endoplasmic reticulum to mitochondria

By O. Brito, L. Scorrano. Nature, 2008

2,382 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/89bc2b3d3d011c5b7ab497e801fb58e4f4db3fb2

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Citations in the corpus

Mitochondrial dysfunction: mechanisms and advances in therapy (2024, background): “85 Endocytosis is a cellular process whereby a vesicle engulfs extracellular material, and it was suggested that transplanted mitochondria can be internalized through this process.”
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability (2011, background): “in a process that depends on the tethering of the mitochondria to the endoplasmic reticulu”
Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation (2011, background): “A prominent role for Mfn1 in effecting mitochondrial fusion during starvation is consistent with evidence implicating Mfn1 as the primary driver of mitochondrial fusion activity, whereasMfn2 has a more diverse set of functions, including responsibility for endoplasmic reticulum– mitochondria tetheri”
Mitochondrial dynamics in mammalian health and disease. (2009, background): “It has been recently reported that Mfn2 (and not Mfn1) is also present in the endoplasmic reticulum (ER) and controls ER morphology and its tethering to mitochondria (72).”
Lipids of mitochondria. (2013, background): “The OMM localized Mfn2 belongs to the family of dynamin-like GTPases and mediates mitochondrial fusion and interaction with Miro (mitochondrial rho GTPase)/Milton complex [289,290].”
Upregulated function of mitochondria-associated ER membranes in Alzheimer disease (2012, positive): “We therefore assayed cholesterol ester and phospholipid synthesis in MEFs lacking mitofusin-2 (Mfn2), a protein that is required for MAM-mediated ER–mitochondrial interactions (de Brito and Scorrano, 2008).”
A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles (2014, background): “A molecular understanding of these contacts has been advanced through studies in yeast and mammalian models (Csordas et al, 1999; de Brito & Scorrano, 2008; Kornmann et al, 2009) and is reviewed elsewhere.”
Importing Mitochondrial Proteins: Machineries and Mechanisms (2009, background): “Relevant to both the role of lipids and the regulation of mitochondrial membrane morphology is the connection between mitochondria and the ER, as components of the mitochondrial fusion machinery are involved in forming proteinaceous ER-mitochondria contact sites (de Brito and Scorrano, 2008).”
Mitochondrial fusion and fission in cell life and death (2010, background): “ER-located MFN2 is engaged in complexes with mitochondrial MFN1 or MFN2, thereby bridging the two organelles and bringing them close together to allow communication by Ca 2+ signallin”
Lipid map of the mammalian cell (2011, background): “The first protein complexes at ER–mitochondria contact sites have been identified (de Brito and Scorrano, 2008; Kornmann et al., 2009).”