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
Summary
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.