ArticleStructure (London, England : 1993)2019
A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- Functional anatomy of zinc finger antiviral protein complexes.Nature communications · 2024Article
- Phosphorylation regulates the chromatin remodeler SMARCAD1 in nucleosome binding, ATP hydrolysis, and histone exchange.The Journal of biological chemistry · 2024Article
- Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism.Cell discovery · 2024Article
- Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.Nature structural & molecular biology · 2023Article
- A SAM-key domain required for enzymatic activity of the Fun30 nucleosome remodeler.Life science alliance · 2023Article
- Targeting NEDD8-activating enzyme for cancer therapy: developments, clinical trials, challenges and future research directions.Journal of hematology & oncology · 2023Review
- Trim28 citrullination maintains mouse embryonic stem cell pluripotency via regulating Nanog and Klf4 transcription.Science China. Life sciences · 2023Article
- TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.Computational and structural biotechnology journal · 2023Article
- Structure and functional mapping of the KRAB-KAP1 repressor complex.The EMBO journal · 2022Article
- Resolving the zinc binding capacity of honey bee vitellogenin and locating its putative binding sites.Insect molecular biology · 2022Article
- Mapping the interaction between Trim28 and the KRAB domain at the center of Trim28 silencing of endogenous retroviruses.Protein science : a publication of the Protein Society · 2022Article
- Arabidopsis CHROMATIN REMODELING 19 acts as a transcriptional repressor and contributes to plant pathogen resistance.The Plant cell · 2022Article
- SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity.Science advances · 2021Article
- Trim24 and Trim33 Play a Role in Epigenetic Silencing of Retroviruses in Embryonic Stem Cells.Viruses · 2020Article
- KRAB domain of ZFP568 disrupts TRIM28-mediated abnormal interactions in cancer cells.NAR cancer · 2020Article
- Resolving the Complexity of Ubiquitin Networks.Frontiers in molecular biosciences · 2020Review
- The Mechanism of Chromatin Remodeler SMARCAD1/Fun30 in Response to DNA Damage.Frontiers in cell and developmental biology · 2020Review
- Nucleosome Remodeling by Fun30Frontiers in molecular biosciences · 2019Review
- Moving Mountains-The BRCA1 Promotion of DNA Resection.Frontiers in molecular biosciences · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Ubiquitylation, the posttranslational linkage of ubiquitin moieties to lysines in target proteins, helps regulate a myriad of biological processes. Ubiquitin, and sometimes ubiquitin-homology domains, are recognized by ubiquitin-binding domains, including CUE domains. CUE domains are thus generally thought to function by mediating interactions with ubiquitylated proteins. The chromatin remodeler, SMARCAD1, interacts with KAP1, a transcriptional corepressor. The SMARCAD1-KAP1 interaction is direct and involves the first SMARCAD1 CUE domain (CUE1) and the RBCC domain of KAP1. Here, we present a structural model of the KAP1 RBCC-SMARCAD1 CUE1 complex based on X-ray crystallography. Remarkably, CUE1, a canonical CUE domain, recognizes a cluster of exposed hydrophobic and surrounding charged/amphipathic residues on KAP1, which are presented in the context of a coiled-coil domain, not in a structure resembling ubiquitin. Together, these data suggest that CUE domains may have a wider function than simply recognizing ubiquitin and the ubiquitin-fold.
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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.