| Literature DB >> 28647376 |
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.Keywords: ATP synthase; Bioenergetics; Dimers; c-subunit ring
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Year: 2017 PMID: 28647376 DOI: 10.1016/j.neuint.2017.06.010
Source DB: PubMed Journal: Neurochem Int ISSN: 0197-0186 Impact factor: 3.921