Eight human OPA1 isoforms, long and short: What are they for?

Valentina Del Dotto, Mario Fogazza, Valerio Carelli, Michela Rugolo, Claudia Zanna

Research output: Contribution to journalReview articlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)263-269
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number4
DOIs
Publication statusPublished - Apr 1 2018

Keywords

  • Cristae
  • Energetics
  • Long and short OPA1 forms
  • Mitochondrial network dynamics
  • mtDNA
  • OPA1

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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