ArticleBiochemical and biophysical research communications2021
Molecular double clips within RepID WD40 domain control chromatin binding and CRL4-substrate assembly.
Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- PHIP suppresses NuRD to enable the growth of SWI/SNF-mutant cancers.Nature communications · 2026Article
- RepID promotes metastatic potential in osteosarcoma through regulation of the PRC1-GATA6 axis.Animal cells and systems · 2026Article
- RepID depletion enhances TWS119-induced erythropoiesis through chromatin reprogramming and transcription factor recruitment.Genes & genomics · 2025Article
- GWAS identifies novel loci linked to seedling growth traits in highly diverse barley population under drought stress.Scientific reports · 2025Article
- Genome-wide identification and analysis of WD40 proteins reveal that NtTTG1 enhances drought tolerance in tobacco (Nicotiana tabacum).BMC genomics · 2024Article
- RepID represses megakaryocytic differentiation by recruiting CRL4A-JARID1A at DAB2 promoter.Cell communication and signaling : CCS · 2023Article
- RepID represses megakaryocytic differentiation by recruiting CRL4A-JARID1A at DAB2 promoter.Research square · 2023Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The cell cycle is modulated by ubiquitin ligases, including CRL4, which facilitate degradation of the chromatin-bound substrates involved in DNA replication and chromosome segregation. One of the members of the CRL4 complex, RepID (DCAF14/PHIP), recognizes kinetochore-localizing BUB3, known as the CRL4 substrate, and recruits CRL4 to the chromatin/chromosome using the WD40 domain. Here, we show that the RepID WD40 domain provides different platforms to CRL4 and BUB3. Deletion of the H-box or exon 8 located in the RepID WD40 domain compromises the interaction between RepID and CRL4, whereas BUB3 interacts with the exon 1-2 region. Moreover, deletion mutants of other exons in the WD40 domain lost chromatin binding affinity. Structure prediction revealed that the RepID WD40 domain has two beta-propeller folds, linked by loops, which are possibly crucial for chromatin binding. These findings provide mechanistic insights into the space occupancy of the RepID WD40 domain to form a complex with CRL4, BUB3, or chromatin.
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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.