ArticleThe Journal of biological chemistry2011
An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Novel therapeutic strategies for targeting fatty acid oxidation in cancer.Biomarker research · 2025Review
- Review
- Ginsenoside Rb1 regulates CPT1A deacetylation to inhibit intramuscular fat infiltration after rotator cuff tear.iScience · 2024Article
- Mitochondrial morphology controls fatty acid utilization by changing CPT1 sensitivity to malonyl-CoA.The EMBO journal · 2023Article
- Metabolic sensing and control in mitochondria.Molecular cell · 2023Review
- To be or not to be a fat burner, that is the question for cpt1c in cancer cells.Cell death & disease · 2023Review
- Mitochondrial CPT1A: Insights into structure, function, and basis for drug development.Frontiers in pharmacology · 2023Review
- Multiomic analysis identifies CPT1A as a potential therapeutic target in platinum-refractory, high-grade serous ovarian cancer.Cell reports. Medicine · 2021Article
- Butyrate enhances CPT1A activity to promote fatty acid oxidation and iTreg differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Sensing of nutrients by CPT1C controls SAC1 activity to regulate AMPA receptor trafficking.The Journal of cell biology · 2020Article
- Sensing of nutrients by CPT1C regulates late endosome/lysosome anterograde transport and axon growth.eLife · 2019Article
- Translocator Protein (TSPO) Affects Mitochondrial Fatty Acid Oxidation in Steroidogenic Cells.Endocrinology · 2016Article
- Mutation in CPT1C Associated With Pure Autosomal Dominant Spastic Paraplegia.JAMA neurology · 2015Article
- Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1.Biopolymers · 2014Article
- Thymidine kinase 2 deficiency-induced mtDNA depletion in mouse liver leads to defect β-oxidation.PloS one · 2013Article
- Construction of covalent membrane protein complexes and high-throughput selection of membrane mimics.Journal of the American Chemical Society · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The enzyme carnitine palmitoyltransferase 1 (CPT1), which is anchored in the outer mitochondrial membrane (OMM), controls the rate-limiting step in fatty acid β-oxidation in mammalian tissues. It is inhibited by malonyl-CoA, the first intermediate of fatty acid synthesis, and it responds to OMM curvature and lipid characteristics, which reflect long term nutrient/hormone availability. Here, we show that the N-terminal regulatory domain (N) of CPT1A can adopt two complex amphiphilic structural states, termed Nα and Nβ, that interchange in a switch-like manner in response to offered binding surface curvature. Structure-based site-directed mutageneses of native CPT1A suggest Nα to be inhibitory and Nβ to be noninhibitory, with the relative Nα/Nβ ratio setting the prevalent malonyl-CoA sensitivity of the enzyme. Based on the amphiphilic nature of N and molecular modeling, we propose malonyl-CoA sensitivity to be coupled to the properties of the OMM by Nα-OMM associations that alter the Nα/Nβ ratio. For enzymes residing at the membrane-water interface, this constitutes an integrative regulatory mechanism of exceptional sophistication.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.