| First Author | Belenguer P | Year | 2013 |
| Journal | Biochim Biophys Acta | Volume | 1833 |
| Issue | 1 | Pages | 176-83 |
| PubMed ID | 22902477 | Mgi Jnum | J:198403 |
| Mgi Id | MGI:5496509 | Doi | 10.1016/j.bbamcr.2012.08.004 |
| Citation | Belenguer P, et al. (2013) The dynamin GTPase OPA1: more than mitochondria?. Biochim Biophys Acta 1833(1):176-83 |
| abstractText | The studies addressing the molecular mechanisms governing mitochondrial fusion and fission have brought to light a small group of dynamin-like GTPases (Guanosine-Triphosphate hydrolase) as central regulators of mitochondrial morphology and cristae remodeling, apoptosis, calcium signaling, and metabolism. One of them is the mammalian OPA1 (Optic atrophy 1) protein, which resides inside the mitochondrion anchored to the inner membrane and, in a cleaved form, is associated to oligomeric complexes, in the intermembrane space of the organelle. Here, we review the studies that have made OPA1 emerge as the best understood regulator of mitochondrial inner membrane fusion and cristae remodeling. Further, we re-examine the findings behind the recent claim that OPA1 mediates adrenergic control of lipolysis by functioning as a cytosolic A-kinase anchoring protein (AKAP), on the hemimembrane that envelops the lipid droplet. This article is part of a Special Issue entitled: Mitochondrial dynamics and physiology. |
