Mic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric F1F0-ATP Synthase

被引：49

作者：

Rampelt, Heike ^{[1
]}

Bohnert, Maria ^{[1
]}

Zerbes, Ralf M. ^{[1
]}

Horvath, Susanne E. ^{[1
]}

Warscheid, Bettina ^{[2
,3
]}

Pfanner, Nikolaus ^{[1
,3
]}

van der Laan, Martin ^{[4
]}

机构：

[1] Univ Freiburg, Inst Biochem & Mol Biol, Fac Med, ZBMZ, D-79104 Freiburg, Germany

[2] Univ Freiburg, Fac Biol, Inst Biol 2, Biochem Funct Prote, D-79104 Freiburg, Germany

[3] Univ Freiburg, BIOSS Ctr Biol Signalling Studies, D-79104 Freiburg, Germany

[4] Saarland Univ, Ctr Mol Signaling, Med Biochem & Mol Biol, PZMS, D-66421 Homburg, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2017年 / 429卷 / 08期

关键词：

mitochondria; MICOS; membrane architecture; inner membrane; cell organelles; ATP SYNTHASE; INNER MEMBRANE; F1FO-ATP SYNTHASE; MICOS COMPLEX; MITOFILIN; YEAST; ORGANIZATION; REVEALS; SAM50; ARCHITECTURE;

D O I：

10.1016/j.jmb.2017.03.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mitochondria! 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 F1F0-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 F1F0-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 F1F0-ATP synthase. (C) 2017 Elsevier Ltd. All rights reserved.

引用

收藏

页码：1162 / 1170

页数：9

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