ArticleThe Journal of biological chemistry2013
Nicotinamide adenine dinucleotide-induced multimerization of the co-repressor CtBP1 relies on a switching tryptophan.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 83 citations in OpenAlex.
- Article
- Obesity Disrupts CtBP2-Mediated Maintenance of Transcriptional Equilibrium in Hypothalamic Feeding Circuitry.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Molecular mechanism of CtBP1-S/BARS-driven membrane fission and its cellular control by metabolic ligands.Science advances · 2026Article
- Metabolic oxidoreductases: central regulators of the epigenetic landscapes in stemness.Experimental & molecular medicine · 2026Review
- CtBP1 sustains activity-dependent muscle properties and dampens synaptic, contractile and metabolic changes triggered by denervation.Skeletal muscle · 2026Article
- NAD(H)-dependent corepressor CTBP1 integrates metabolic signals to drive oncogenic programs.Frontiers in immunology · 2026Review
- The secreted metabolite sensor CtBP2 links metabolism to healthy lifespan.Nature aging · 2025Article
- Analytical Post-Embedding Immunogold-Electron Microscopy with Direct Gold-Labelled Monoclonal Primary Antibodies against RIBEYE A- and B-Domain Suggests a Refined Model of Synaptic Ribbon Assembly.International journal of molecular sciences · 2024Article
- Master corepressor inactivation through multivalent SLiM-induced polymerization mediated by the oncogene suppressor RAI2.Nature communications · 2024Article
- Identification and characterization of a new potent inhibitor targeting CtBP1/BARS in melanoma cells.Journal of experimental & clinical cancer research : CR · 2024Article
- A regulatory role for the unstructured C-terminal domain of the CtBP transcriptional corepressor.The Journal of biological chemistry · 2024Article
- A regulatory role for the unstructured C-terminal domain of the CtBP transcriptional corepressor.bioRxiv : the preprint server for biology · 2023Article
- The Cynosure of CtBP: Evolution of a Bilaterian Transcriptional Corepressor.Molecular biology and evolution · 2023Article
- Inhibition of CtBP-Regulated Proinflammatory Gene Transcription Attenuates Psoriatic Skin Inflammation.The Journal of investigative dermatology · 2022Article
- RIBEYE B-Domain Is Essential for RIBEYE A-Domain Stability and Assembly of Synaptic Ribbons.Frontiers in molecular neuroscience · 2022Article
- The transcriptional corepressor CtBP2 serves as a metabolite sensor orchestrating hepatic glucose and lipid homeostasis.Nature communications · 2021Article
- Chemical Proteomics Approach for Profiling the NAD Interactome.Journal of the American Chemical Society · 2021Article
- Tête-à-tête with CtBP dimers.Structure (London, England : 1993) · 2021Article
- Cryo-EM structure of CtBP2 confirms tetrameric architecture.Structure (London, England : 1993) · 2021Article
- C-terminal binding proteins 1 and 2 in traumatic brain injury-induced inflammation and their inhibition as an approach for anti-inflammatory treatment.International journal of biological sciences · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The transcriptional co-repressor C-terminal binding protein (CtBP) interacts with a number of repressor proteins and chromatin modifying enzymes. How the biochemical properties including binding of dinucleotide, oligomerization, and dehydrogenase domains of CtBP1 direct the assembly of a functional co-repressor to influence gene expression is not well understood. In the current study we demonstrate that CtBP1 assembles into a tetramer in a NAD(H)-dependent manner, proceeding through a dimeric intermediate. We find that NAD-dependent oligomerization correlates with NAD(+) binding affinity and that the carboxyl terminus is required for assembly of a dimer of dimers. Mutant CtBP1 proteins that abrogate dinucleotide-binding retain wild type affinity for the PXDLS motif, but do not self-associate either in vitro or in vivo. CtBP1 proteins with mutations in the dehydrogenase domain still retain the ability to self-associate and bind target proteins. Both co-immunoprecipitation and mammalian two-hybrid experiments demonstrate that CtBP1 self-association occurs within the nucleus, and depends on dinucleotide binding. Repression of transcription does not depend on dinucleotide binding or an intact dehydrogenase domain, but rather depends on the amino-terminal domain that recruits PXDLS containing targets. We show that tryptophan 318 (Trp(318)) is a critical residue for tetramer assembly and likely functions as a switch for effective dimerization following NAD(+) binding. These results suggest that dinucleotide binding permits CtBP1 to form an intranuclear homodimer through a Trp(318) switch, creating a nucleation site for multimerization through the C-terminal domain for tetramerization to form an effective repression complex.
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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.