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IF1 通过抑制线粒体 ATP 酶的功能改变 ATP 合酶的时空组织。

Inhibition of the mitochondrial ATPase function by IF1 changes the spatiotemporal organization of ATP synthase.

机构信息

Center of Cellular Nanoanalytics, Integrated Bioimaging Facility, University of Osnabrück, 49076 Osnabrück, Lower Saxony, Germany.

Institute of Molecular Cell Biology, Department of Biology, University of Muenster, 48149 Muenster, Germany.

出版信息

Biochim Biophys Acta Bioenerg. 2021 Jan 1;1862(1):148322. doi: 10.1016/j.bbabio.2020.148322. Epub 2020 Oct 14.

DOI:10.1016/j.bbabio.2020.148322
PMID:33065099
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7718977/
Abstract

• Mitochondrial FF ATP synthase is the key enzyme for mitochondrial bioenergetics. Dimeric FF-ATP synthase, is preferentially located at the edges of the cristae and its oligomerization state determines mitochondrial ultrastructure. The ATP synthase inhibitor protein IF1 modulates not only ATP synthase activity but also regulates both the structure and function of mitochondria. In order to understand this in more detail, we have investigated the effect of IF1 on the spatiotemporal organization of the ATP synthase. Stable cell lines were generated that overexpressed IF1 and constitutively active IF1-H49K. The expression of IF1-H49K induced a change in the localization and mobility of the ATP synthase as analyzed by single molecule tracking and localization microscopy (TALM). In addition, the ultrastructure and function of mitochondria in cells with higher levels of active IF1 displayed a gradual alteration. In state III, cristae structures were significantly altered. The inhibition of the hydrolase activity of the FF-ATP synthase by IF1 together with altered inner mitochondrial membrane caused re-localization and altered mobility of the enzyme.

摘要

• 线粒体 FF ATP 合酶是线粒体生物能量学的关键酶。二聚体 FF-ATP 合酶优先位于嵴的边缘，其寡聚状态决定了线粒体的超微结构。ATP 合酶抑制剂蛋白 IF1 不仅调节 ATP 合酶的活性，还调节线粒体的结构和功能。为了更详细地了解这一点，我们研究了 IF1 对 ATP 合酶时空组织的影响。生成了稳定的细胞系，过表达 IF1 和组成型激活的 IF1-H49K。通过单分子追踪和定位显微镜（TALM）分析，IF1-H49K 的表达诱导了 ATP 合酶定位和迁移率的变化。此外，具有更高活性 IF1 水平的细胞中线粒体的超微结构和功能显示出逐渐改变。在状态 III 中，嵴结构发生了显著改变。IF1 与改变的线粒体内膜一起抑制 FF-ATP 合酶的水解酶活性，导致酶的重新定位和迁移率改变。

相似文献

[1]
Inhibition of the mitochondrial ATPase function by IF1 changes the spatiotemporal organization of ATP synthase.

Biochim Biophys Acta Bioenerg. 2021-1-1

[2]
The spatio-temporal organization of mitochondrial FF ATP synthase in cristae depends on its activity mode.

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[3]
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[2]
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[3]
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[4]
The homolog of ATPase inhibitory factor 1 is critical for mitochondrial cristae maintenance and stress response.

Mol Biol Cell. 2025-1-1

[5]
The homolog of ATPase inhibitory factor 1 is critical for mitochondrial cristae maintenance and stress response.

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[6]
Mitochondrial F0F1-ATP synthase governs the induction of mitochondrial fission.

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[7]
Mitochondrial membrane potential regulates nuclear DNA methylation and gene expression through phospholipid remodeling.

bioRxiv. 2024-1-13

[8]
IF1 promotes oligomeric assemblies of sluggish ATP synthase and outlines the heterogeneity of the mitochondrial membrane potential.

Commun Biol. 2023-8-12

[9]
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[10]
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本文引用的文献

[1]
Optimization of highly inclined illumination for diffraction-limited and super-resolution microscopy.

Opt Express. 2023-7-31

[2]
Mitochondrial F-ATP synthase as the permeability transition pore.

Pharmacol Res. 2020-10

[3]
Quantification of cristae architecture reveals time-dependent characteristics of individual mitochondria.

Life Sci Alliance. 2020-7

[4]
Shaping the mitochondrial inner membrane in health and disease.

J Intern Med. 2020-2-26

[5]
The spatio-temporal organization of mitochondrial FF ATP synthase in cristae depends on its activity mode.

Biochim Biophys Acta Bioenerg. 2019-11-27

[6]
Individual cristae within the same mitochondrion display different membrane potentials and are functionally independent.

EMBO J. 2019-10-14

[7]
Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1.

Nature. 2019-7-10

[8]
Mitochondrial cristae narrowing upon higher 2-oxoglutarate load.

Biochim Biophys Acta Bioenerg. 2019-6-25

[9]
Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.

Science. 2019-6-14

[10]
Extrinsic conditions influence the self-association and structure of IF, the regulatory protein of mitochondrial ATP synthase.

Proc Natl Acad Sci U S A. 2019-5-7

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