Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether
| Autor: | Marta Giacomello, Martina Semenzato, Luca Scorrano, Marta Zaninello, Diego De Stefani, María Isabel Hernández-Alvarez, Tatiana Varanita, Gerald W. Dorn, Annalisa Serafini, Sowmya Lakshminaranayan, Deborah Naon, Francesca Grespi, Antonio Zorzano, Stéphanie Herkenne |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
MFN2 Tethering Mitochondrion Biology Endoplasmic Reticulum GTP Phosphohydrolases 03 medical and health sciences Mitofusin-2 0302 clinical medicine Organelle Human Umbilical Vein Endothelial Cells Animals Humans Letters Uptake rate Interorganellar communication Mice Knockout Ca2+ Mfn2 Mitochondria Multidisciplinary Endoplasmic reticulum Mitochondrial calcium uniporter Fibroblasts Biological Sciences Embryo Mammalian Cell biology 030104 developmental biology Liver Biochemistry Molecular Probes Calcium Calcium Channels Gene Deletion 030217 neurology & neurosurgery Function (biology) |
| Popis: | Significance Organelles engage in heterotypic interactions crucial for metabolic and signaling cascades. The best-studied case of this heterotypic interaction is that between the mitochondria and endoplasmic reticulum (ER), crucial for transfer of lipids and especially Ca 2+ between the two organelles. The original discovery that the mitochondria-shaping protein Mitofusin 2 (Mfn2) physically tethers the ER to mitochondria was recently challenged. Here, electron microscopy and fluorescent probes of organelle proximity provide definitive evidence that constitutive or acute Mfn2 ablation increases the distance between the ER and mitochondria. Functionally, this process reduces mitochondrial Ca 2+ uptake without altering the mitochondrial Ca 2+ uniporter complex in multiple tissues. Thus, the discoveries of the role of ER–mitochondria juxtaposition in cell biology based on Mfn2 as a tool remain unchallenged. |
| Databáze: | OpenAIRE |
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