Acetyl‐CoA carboxylase isoforms: polymerization and formation of multi‐protein complexes
Bibliographic record
Abstract
Mammalian acetyl‐CoA carboxylase (ACC) isoforms, ACC‐1 and ACC‐2, catalyze the formation of malonyl‐CoA, a substrate for fatty acid synthesis and fatty acyl chain elongation, and a potent inhibitor of beta‐oxidation. Based on the phenotype of knockout mice, ACC contributes significantly to overall body energy metabolism and is a potential drug target for the treatment of obesity and type II diabetes. Highly‐purified ACC‐1 undergoes a dramatic increase in mass following treatment with allosteric activators such as citrate, apparently due to linear polymerization of ACC dimers. The current studies were undertaken to explore (a) the extent to which ACC‐2 undergoes polymerization and (b) to investigate whether other cellular proteins associate with and perhaps regulate the polymerization process. Size exclusion chromatography and sucrose gradient sedimentation studies show that ACC‐2 undergoes very modest changes in molecular size upon allosteric activation, although the extent of polymerization of ACC‐2 is enhanced in the presence of ACC‐1. Isolation of the largest molecular forms of ACC, followed by mass spectrometry analysis, reveals that ACC “polymers” are multi‐protein complexes. The proteins most reliably detected in ACC polymer fractions include tubulin, actin, fatty acid synthase, and heat shock proteins. The significance of the additional components of ACC complexes is evaluated from effects on the kinetics of the ACC reaction and of the polymerization process, as well as by cellular co‐localization using fluorescence microscopy and co‐immunoprecipitation studies. These studies were supported by a grant from the Canadian Institutes of Health Research.
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| 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 | 0.001 | 0.001 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.001 |
| Insufficient payload (model declined to judge) | 0.001 | 0.001 |
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 source (direct Gemma or distilled Codex), 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".