Mitochondrial OPA1 cleavage is reversibly activated by differentiation of H9c2 cardiomyoblasts.

ABSTRACT: Optic atrophy-1 (OPA1) is a dynamin-like GTPase localized to the mitochondrial inner membrane, playing key roles in inner membrane fusion and cristae maintenance. OPA1 is regulated by the mitochondrial transmembrane potential (Δψ_m): when Δψ_m is intact, long OPA1 isoforms (L-OPA1) carry out inner membrane fusion. Upon loss of Δψ_m, L-OPA1 isoforms are proteolytically cleaved to short (S-OPA1) isoforms by the stress-inducible OMA1 metalloprotease, causing collapse of the mitochondrial network and promoting apoptosis. Here, we show that L-OPA1 isoforms of H9c2 cardiomyoblasts are retained under loss of Δψ_m, despite the presence of OMA1. However, when H9c2s are differentiated to a more cardiac-like phenotype via treatment with retinoic acid (RA) in lo

SUBMITTER: Garcia I 

PROVIDER: S-EPMC7904612 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature