| First Author | de Brito OM | Year | 2008 |
| Journal | Nature | Volume | 456 |
| Issue | 7222 | Pages | 605-10 |
| PubMed ID | 19052620 | Mgi Jnum | J:142044 |
| Mgi Id | MGI:3820332 | Doi | 10.1038/nature07534 |
| Citation | de Brito OM, et al. (2008) Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456(7222):605-10 |
| abstractText | Juxtaposition between endoplasmic reticulum (ER) and mitochondria is a common structural feature, providing the physical basis for intercommunication during Ca(2+) signalling; yet, the molecular mechanisms controlling this interaction are unknown. Here we show that mitofusin 2, a mitochondrial dynamin-related protein mutated in the inherited motor neuropathy Charcot-Marie-Tooth type IIa, is enriched at the ER-mitochondria interface. Ablation or silencing of mitofusin 2 in mouse embryonic fibroblasts and HeLa cells disrupts ER morphology and loosens ER-mitochondria interactions, thereby reducing the efficiency of mitochondrial Ca(2+) uptake in response to stimuli that generate inositol-1,4,5-trisphosphate. An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of mitochondria. Thus, mitofusin 2 tethers ER to mitochondria, a juxtaposition required for efficient mitochondrial Ca(2+) uptake. |
