ArticleCell cycle (Georgetown, Tex.)2008
Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites.
Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- The splicing factor CCAR1 regulates the Fanconi anemia/BRCA pathway.Molecular cell · 2024Article
- Multifaceted roles of CCAR family proteins in the DNA damage response and cancer.Experimental & molecular medicine · 2024Review
- CCAR-1 works together with the U2AF large subunit UAF-1 to regulate alternative splicing.RNA biology · 2024Article
- SUMO1-regulated DBC1 promotes p53-dependent stress-induced apoptosis of lens epithelial cells.Aging · 2023Article
- Mechanistic insights into the dual role of CCAR2/DBC1 in cancer.Experimental & molecular medicine · 2023Review
- Jumbo Phages: A Comparative Genomic Overview of Core Functions and Adaptions for Biological Conflicts.Viruses · 2021Article
- Deleted in breast cancer 1 as a potential prognostic biomarker in human cancers: a pooled analysis of 2,254 patients.OncoTargets and therapy · 2019Article
- Deleted in Breast Cancer 1 as a Novel Prognostic Biomarker for Digestive System Cancers: A Meta-Analysis.Journal of Cancer · 2019Article
- An Insulin-Responsive Sensor in the SIRT1 Disordered Region Binds DBC1 and PACS-2 to Control Enzyme Activity.Molecular cell · 2018Article
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- A conserved NADScience (New York, N.Y.) · 2017Article
- Article
- The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL.The Journal of cell biology · 2016Article
- DBC1 functions as a tumor suppressor by regulating p53 stability.Cell reports · 2015Article
- DBC1/CCAR2 and CCAR1 Are Largely Disordered Proteins that Have Evolved from One Common Ancestor.BioMed research international · 2014Article
- Deleted in breast cancer-1 (DBC-1) in the interface between metabolism, aging and cancer.Bioscience reports · 2013Review
- Cell cycle and apoptosis regulatory protein (CARP)-1 is expressed in osteoblasts and regulated by PTH.Biochemical and biophysical research communications · 2013Article
- A Functional Proteomics Perspective of DBC1 as a Regulator of Transcription.Journal of proteomics & bioinformatics · 2013Article
- Antagonists of anaphase-promoting complex (APC)-2-cell cycle and apoptosis regulatory protein (CARP)-1 interaction are novel regulators of cell growth and apoptosis.The Journal of biological chemistry · 2011Article
- Reciprocal roles of DBC1 and SIRT1 in regulating estrogen receptor α activity and co-activator synergy.Nucleic acids research · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Deleted in Breast Cancer-1 (DBC1) and its paralog CARP-1 are large multi-domain proteins, with a nuclear or perinuclear localization, and a role in promoting apoptosis upon processing by caspases. Recent studies on human DBC1 show that it is a specific inhibitor of the sirtuin-type deacetylase, Sirt1, which deacetylates histones and p53. Using sensitive sequence profile searches and HMM-HMM comparisons we show that the central conserved globular domain present in the DBC1 and it homologs from diverse eukaryotes is a catalytically inactive version of the Nudix hydrolase (MutT) domain. Given that Nudix domains are known to bind nucleoside diphosphate sugars and NAD, we predict that this domain in DBC1 and its homologs binds NAD metabolites such as ADP-ribose. Hence, we propose that DBC1 and its homologs are likely to regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction. The complex domain architectures of the members of the DBC1 family, which include fusions to the RNA-binding S1-like domain, the DNA-binding SAP domain and EF-hand domains, suggest that they are likely to function as integrators of distinct regulatory signals including chromatin protein modification, soluble compounds in NAD metabolism, apoptotic stimuli and RNA recognition.
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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.