Mic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric F1Fo-ATP Synthase. Issue 8 (21st April 2017)

• Record Type: Journal Article
• Authors: Rampelt, Heike; Bohnert, Maria; Zerbes, Ralf M.; Horvath, Susanne E.; Warscheid, Bettina; Pfanner, Nikolaus; van der Laan, Martin
• Is Part Of: Journal of molecular biology. Volume 429:Issue 8(2017)
• Page Start: 1162
• Page End: 1170
• Publication Date: 2017-04-21
• Subjects: MICOS mitochondrial contact site and cristae organizing system -- Mic10 mitochondrial contact site and cristae organizing system subunit of 10 kDa -- Mic60 mitochondrial contact site and cristae organizing system subunit of ~ 60 kDa (mitofilin/Fcj1) -- Su e subunit e (Atp21/Tim11) of the F1Fo-ATP synthase -- Su g subunit g (Atp20) of the F1Fo-ATP synthase -- F1γ γ subunit of the F1Fo-ATP synthase -- F1β β subunit of the F1Fo-ATP synthase -- Su k subunit k (Atp19) of the F1Fo-ATP synthase -- V/V2/VO monomeric/dimeric/oligomeric forms of the F1Fo-ATP synthase (complex V); mitochondria -- MICOS -- membrane architecture -- inner membrane -- cell organelles; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2017.03.006
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: The mitochondrial contact site and cristae organizing system (MICOS) is crucial for maintaining the architecture of the mitochondrial inner membrane. MICOS is enriched at crista junctions that connect the two inner membrane domains: inner boundary membrane and cristae membrane. MICOS promotes the formation of crista junctions, whereas the oligomeric F1 Fo -ATP synthase is crucial for shaping cristae rims, indicating antagonistic functions of these machineries in organizing inner membrane architecture. We report that the MICOS core subunit Mic10, but not Mic60, binds to the F1 Fo -ATP synthase. Mic10 selectively associates with the dimeric form of the ATP synthase and supports the formation of ATP synthase oligomers. Our results suggest that Mic10 plays a dual role in mitochondrial inner membrane architecture. In addition to its central function in sculpting crista junctions, a fraction of Mic10 molecules interact with the cristae rim-forming F1 Fo -ATP synthase. Graphical Abstract: Highlights: Dual function of Mic10 of mitochondrial contact site and cristae organizing system Mic10 interacts with the dimeric form of mitochondrial F1 Fo -ATP synthase. Mic10 supports the formation of larger oligomers of ATP synthase. Mic10 mediates the functional crosstalk between MICOS and F1 Fo -ATP synthase.