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

Boominathan Amutha; Donna M. Gordon; Yajuan Gu; Debkumar Pain

doi:10.1042/BJ20040566

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

Boominathan Amutha, Donna M. Gordon, Yajuan Gu, Debkumar Pain

Research output: Contribution to journal › Article › peer-review

65 Scopus citations

Abstract

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 F₁F_o-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.

Original language	English (US)
Pages (from-to)	19-23
Number of pages	5
Journal	Biochemical Journal
Volume	381
Issue number	1
DOIs	https://doi.org/10.1042/BJ20040566
State	Published - Jul 1 2004

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

Keywords

ATP synthase
Cytochrome c
Mgm1p
Mitochondria
Rhomboid-like protease
Tim11p

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10.1042/BJ20040566

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

abstract = "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.",

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T1 - A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance

AU - Amutha, Boominathan

AU - Gordon, Donna M.

AU - Gu, Yajuan

AU - Pain, Debkumar

PY - 2004/7/1

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AB - 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.

KW - ATP synthase

KW - Cytochrome c

KW - Mgm1p

KW - Mitochondria

KW - Rhomboid-like protease

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

Abstract

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