A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance

被引:66
作者
Amutha, B [1 ]
Gordon, DM [1 ]
Gu, YJ [1 ]
Pain, D [1 ]
机构
[1] UMDNJ, New Jersey Med Sch, Dept Physiol & Pharmacol, Newark, NJ 07101 USA
关键词
ATP synthase; cytochrome c; Mgm1p; mitochondria; rhomboid-like protease; Tim11p;
D O I
10.1042/BJ20040566
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
In Saccharomyces cerevisiae, two mitochondrial inner-membrane proteins play critical roles in organellar morphology. One is a dynamin-related GTPase, Mgm1p, which participates in mitochondrial fusion. Another is Tim11p, which is required for oligomeric assembly of F1Fo-ATP synthase, which generates ATP through oxidative phosphorylation. Our data bring these findings together and define a novel role for Mgm1p in the formation and maintenance of mitochondrial cristae. We show that Mgm1p serves as an upstream regulator of Tim11p protein stability, ATP synthase assembly, cristae morphology and cytochrome c storage within cristae.
引用
收藏
页码:19 / 23
页数:5
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