Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1859, Issue 4, Pages 263-269Publisher
ELSEVIER
DOI: 10.1016/j.bbabio.2018.01.005
Keywords
OPA1; Long and short OPA1 forms; Mitochondrial network dynamics; Cristae; mtDNA; Energetics
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Funding
- FIR grant from the Ministero della Istruzione University e Ricerca (MIUR) [RBFR131WDS]
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OPA1 is a dynamin-related GTPase that controls mitochondrial dynamics, cristae integrity, energetics and mtDNA maintenance. The exceptional complexity of this protein is determined by the presence, in humans, of eight different isoforms that, in turn, are proteolytically cleaved into combinations of membrane-anchored long forms and soluble short forms. Recent advances highlight how each OPA1 isoform is able to fulfill essential mitochondrial functions, whereas only some variants carry out specialized features. Long forms determine fusion, long or short forms alone build cristae, whereas long and short forms together tune mitochondrial morphology. These findings offer novel challenging therapeutic potential to gene therapy.
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