Interconnected roles of mitochondrial carrier proteins ANT, PiT, and UCPs in proton transport
Bibliographic record
Abstract
Introduction Adenine nucleotide translocase (ANT), phosphate translocase (P i T), and uncoupling proteins (UCPs), all integral to oxidative phosphorylation, are among the carrier proteins of the mitochondrial inner membrane (MIM). While traditionally thought to function as monomers, their close proximity within the densely packed MIM suggests potential mutual interactions and formation of homo- and/or hetero-oligomers, the physiological implications of which are yet to be understood. Methods We investigated the conformations and proton transport activity of ANT1, P i T, UCP2 and UCP4 individually and in combination, to explore the possibility of hetero-oligomerization and functionally relevant interactions among the proteins. Monomeric proteins were reconstituted, individually and/or in combination, into model lipid membranes and the conformation, oligomeric state, and proton transport activities were assessed using biophysical approaches. Results UCP2 and UCP4 spontaneously assembled into functional tetramers, whereas ANT1 and P i T predominantly remained monomeric. The presence of cardiolipin in lipid membranes affected ANT1 oligomerization but had no influence on UCPs or P i T, suggesting that homotetramerization may be a characteristic of only a subset of mitochondrial carriers. Nevertheless, binary and ternary combinations of the proteins formed heterotetramers capable of proton transport. The UCP2-ANT1 combination showed significant proton transport, whereas proton transport by the UCP4-P i T combination was substantially lower, highlighting the specificity of interactions. Proton transport was differentially activated by free fatty acids; oleic acid was a better activator than palmitic acid. Inhibitory effects of purine nucleotides also varied across different protein combinations. Discussion Collectively, our findings emphasize how interactions among these four mitochondrial carrier proteins may affect proton transport across the MIM and influence mitochondrial bioenergetics.
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How this classification was reachedexpand
Full frame distilled prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.
Codex and Gemma teacher scores by category
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one teacher head, not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".