Mitochondrial permeability transition pore: Back to the drawing board


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Abstract

Current models theorizing on what the mitochondrial permeability transition (mPT) pore is made of, implicate the c-subunit rings of ATP synthase complex. However, two very recent studies, one on atomistic simulations and in the other disrupting all genes coding for the c subunit disproved those models. As a consequence of this, the structural elements of the pore remain unknown. The purpose of the present short-review is to (i) briefly review the latest findings, (ii) serve as an index for more comprehensive reviews regarding mPT specifics, (iii) reiterate on the potential pitfalls while investigating mPT in conjunction to bioenergetics, and most importantly (iv) suggest to those in search of mPT pore identity, to also look elsewhere.HIGHLIGHTSc-subunit ring was proposed to form mPT structure, disproved by two recent studies.These two studies are reviewed.Bioenergetic pitfalls regarding mPT protocols are reiterated.Alternative approaches for identifying mPT structure are reviewed.

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