| Background | Dynamin-like GTPase OPA1, mitochondrial is a ~111 kDa protein. Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase OPA1, long form; L-OPA1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-OPA1 and S-OPA1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-OPA1 and S-OPA1 is essential: excess levels of S-OPA1, produced by cleavage by OMA1 following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, inhibiting mitochondrial fusion. The balance between L-OPA1 and S-OPA1 also influences cristae shape and morphology. 1. Ishihara, N. et al. (2006) The EMBO journal 25, 2966-77. PMID: 167787702. Song, Z. et al. (2007) The Journal of cell biology 178, 749-55. PMID: 177094293. Ban, T. et al. (2010) Human molecular genetics 19, 2113-22. PMID: 201855554. Anand, R. et al. (2014) The Journal of cell biology 204, 919-29. PMID: 246162255. Ban, T. et al. (2017) Nature cell biology 19, 856-863. PMID: 286280839. Stephan, T. et al. (2020) The EMBO journal 39, e104105. PMID: 32567732 |
|---|
中文
English
한국어
日本語
Español
Français
Русский
