%0 Journal Article %1 rampeltMic10CoreSubunit2017 %A Rampelt, Heike %A Bohnert, Maria %A Zerbes, Ralf M. %A Horvath, Susanne E. %A Warscheid, Bettina %A Pfanner, Nikolaus %A van der Laan, Martin %C Netherlands %D 2017 %J Journal of molecular biology %K ATPases/genetics/*metabolism,Protein Multimerization,Protein Proteins/genetics/*metabolism,MICOS,mitochondria,Mitochondria/metabolism,Mitochondrial Proteins/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,to_read Proton-Translocating Transport,Saccharomyces architecture,Membrane cell cerevisiae membrane,membrane organelles,inner %N 8 %P 1162--1170 %R 10.1016/j.jmb.2017.03.006 %T Mic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric F(1)F(o)-ATP Synthase. %V 429 %X 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 F(1)F(o)-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 F(1)F(o)-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 F(1)F(o)-ATP synthase.

@article{rampeltMic10CoreSubunit2017, 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 F(1)F(o)-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 F(1)F(o)-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 F(1)F(o)-ATP synthase.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {Netherlands}, author = {Rampelt, Heike and Bohnert, Maria and Zerbes, Ralf M. and Horvath, Susanne E. and Warscheid, Bettina and Pfanner, Nikolaus and {van der Laan}, Martin}, biburl = {https://www.bibsonomy.org/bibtex/24923e2186c58ea3c80dc50f48763524f/warscheidlab}, copyright = {Copyright {\copyright} 2017 Elsevier Ltd. All rights reserved.}, doi = {10.1016/j.jmb.2017.03.006}, interhash = {534ada41beda725630ee0374aeea92bc}, intrahash = {4923e2186c58ea3c80dc50f48763524f}, issn = {1089-8638 0022-2836}, journal = {Journal of molecular biology}, keywords = {ATPases/genetics/*metabolism,Protein Multimerization,Protein Proteins/genetics/*metabolism,MICOS,mitochondria,Mitochondria/metabolism,Mitochondrial Proteins/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,to_read Proton-Translocating Transport,Saccharomyces architecture,Membrane cell cerevisiae membrane,membrane organelles,inner}, langid = {english}, month = apr, number = 8, pages = {1162--1170}, pmid = {28315355}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Mic10, a {{Core Subunit}} of the {{Mitochondrial Contact Site}} and {{Cristae Organizing System}}, {{Interacts}} with the {{Dimeric F}}(1){{F}}(o)-{{ATP Synthase}}.}, volume = 429, year = 2017 }