The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes

Suzanne Hoppins, Frank Edlich, Megan M. Cleland, Soojay Banerjee, J. Michael McCaffery, Richard J. Youle, Jodi Nunnari

Research output: Contribution to journalArticle

130 Scopus citations

Abstract

In mammals, fusion of the mitochondrial outer membrane is controlled by two DRPs, MFN1 and MFN2, that function in place of a single outer membrane DRP, Fzo1 in yeast. We addressed the significance of two mammalian outer membrane fusion DRPs using an in vitro mammalian mitochondrial fusion assay. We demonstrate that heterotypic MFN1-MFN2 trans complexes possess greater efficacy in fusion as compared to homotypic MFN1 or MFN2 complexes. In addition, we show that the soluble form of the proapoptotic Bcl2 protein, Bax, positively regulates mitochondrial fusion exclusively through homotypic MFN2 trans complexes. Together, these data demonstrate functional and regulatory distinctions between MFN1 and MFN2 and provide insight into their unique physiological roles.

Original languageEnglish (US)
Pages (from-to)150-160
Number of pages11
JournalMolecular Cell
Volume41
Issue number2
DOIs
StatePublished - Jan 21 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Hoppins, S., Edlich, F., Cleland, M. M., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. (2011). The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes. Molecular Cell, 41(2), 150-160. https://doi.org/10.1016/j.molcel.2010.11.030