ArticleProceedings of the National Academy of Sciences of the United States of America2003
Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
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.
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Who cites it
54 citing papers in PubMed, 143 citations in OpenAlex.
- Protein-Protein Interactions in Base Excision Repair.Biomolecules · 2025Review
- Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation.International journal of molecular sciences · 2024Review
- Single Nucleotide Polymorphisms (SNPs) in the Shadows: Uncovering their Function in Non-Coding Region of Esophageal Cancer.Current pharmaceutical biotechnology · 2024Review
- The diagnostic or prognostic values of FADD in cancers based on pan‑cancer analysis.Biomedical reports · 2023Article
- A Dual Role for FADD in Human Precursor T-Cell Neoplasms.International journal of molecular sciences · 2022Article
- Caspase-8 and FADD prevent spontaneous ZBP1 expression and necroptosis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Mechanisms of Genome Maintenance in Plants: Playing It Safe With Breaks and Bumps.Frontiers in genetics · 2021Review
- Long non-coding RNA regulation of TRAIL in breast cancer: A tangle of non-coding threads.Oncology letters · 2020Review
- Review
- Article
- Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets.Genes · 2017Review
- MBD4 Facilitates Immunoglobulin Class Switch Recombination.Molecular and cellular biology · 2017Article
- Article
- Effects of anti-depressant treatments on FADD and p-FADD protein in rat brain cortex: enhanced anti-apoptotic p-FADD/FADD ratio after chronic desipramine and fluoxetine administration.Psychopharmacology · 2016Article
- The Mbd4 DNA glycosylase protects mice from inflammation-driven colon cancer and tissue injury.Oncotarget · 2016Article
- MBD4 interacts with and recruits USP7 to heterochromatic foci.Journal of cellular biochemistry · 2015Article
- The role of death-associated protein 3 in apoptosis, anoikis and human cancer.Cancer cell international · 2015Article
- MBD4 cooperates with DNMT1 to mediate methyl-DNA repression and protects mammalian cells from oxidative stress.Epigenetics · 2014Article
- The Drosophila IMD pathway in the activation of the humoral immune response.Developmental and comparative immunology · 2014Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Fas-associated death domain protein (FADD) is an adaptor protein bridging death receptors with initiator caspases. Thus, its function and localization are assumed to be cytoplasmic, although the localization of endogenous FADD has not been reported. Surprisingly, the data presented here demonstrate that FADD is mainly nuclear in several adherent cell lines. Its accumulation in the nucleus and export to the cytoplasm required the phosphorylation site Ser-194, which was also required for its interaction with the nucleocytoplasmic shuttling protein exportin-5. Within the nucleus, FADD interacted with the methyl-CpG binding domain protein 4 (MBD4), which excises thymine from GT mismatches in methylated regions of chromatin. The MBD4-interacting mismatch repair factor MLH1 was also found in a complex with FADD. The FADD-MBD4 interaction involved the death effector domain of FADD and a region of MBD4 adjacent to the glycosylase domain. The FADD-binding region of MBD4 was downstream of a frameshift mutation that occurs in a significant fraction of human colorectal carcinomas. Consistent with the idea that MBD4 can signal to an apoptotic effector, MBD4 regulated DNA damage-, Fas ligand-, and cell detachment-induced apoptosis. The nuclear localization of FADD and its interaction with a genome surveillance/DNA repair protein that can regulate apoptosis suggests a novel function of FADD distinct from direct participation in death receptor signaling complexes.
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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.