Identification of new OPA1 cleavage site reveals that short isoforms regulate mitochondrial fusion
Ruohan Wang, Prashant Mishra, Spiros D. Garbis, Annie Moradian, Michael J. Sweredoski, David C. Chan
Abstract
locus no longer produces transcripts with S2 cleavage sites, we generated a simplified system to identify the new YME1L-dependent site S3 that mediates constitutive and complete cleavage of OPA1. We show that mitochondrial morphology is highly sensitive to the ratio of l-OPA1 to s-OPA1, indicating that s-OPA1 regulates mitochondrial fusion.
Topics & Concepts
Biologymitochondrial fusionDynaminGene isoformCell biologyMediatorMitochondrionTranslocase of the inner membraneGTPaseCleavage (geology)Inner mitochondrial membraneLipid bilayer fusionMitochondrial carrierGeneticsGeneMitochondrial DNABacterial outer membraneMitochondrial membrane transport proteinMembraneReceptorFracture (geology)PaleontologyEscherichia coliEndocytosisMitochondrial Function and PathologyATP Synthase and ATPases ResearchMetabolism and Genetic Disorders