Abstract

What makes you can also break you: mitochondrial permeability transition pore formation by the c subunit of the F1F0 ATP-synthase?

Highlights

  • A number of cellular stresses and cytotoxic agents trigger mitochondrial permeability transition, considered as a final common pathway of cell death (Brenner and Grimm, 2006). mPT follows the formation of a large non-selective pore in the inner membrane of mitochondria (IMM), permeable to molecules up to 1.5 kD

  • These results imply that a conformational change of the c-ring might transform it to a nonselective pore, presenting a provocative idea leading to a series of outstanding questions

  • Separating the consequent bioenergetic effects from the direct molecular consequences of c subunit knockdown is essentially unworkable. The authors addressed this issue by silencing the catalytic F1-localized α subunit as a control, which had no effect on mPT, while the genetic manipulation should have had the same impact on the number of functional F1F0 ATP-synthases

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Summary

Introduction

A number of cellular stresses and cytotoxic agents trigger mitochondrial permeability transition (mPT), considered as a final common pathway of cell death (Brenner and Grimm, 2006). mPT follows the formation of a large non-selective pore (mPTP) in the inner membrane of mitochondria (IMM), permeable to molecules up to 1.5 kD. The rotation of the membrane-embedded ring formed by the c subunits of the ATP-synthase is driven by the proton motive force across the IMM.

Results
Conclusion

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