ReviewNucleus (Austin, Tex.)2015
Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1.
Review in Nucleus (Austin, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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
23 citing papers in PubMed, 34 citations in OpenAlex.
- Natural and Synthetic Anticancer Epidrugs Targeting the Epigenetic Integrator UHRF1.Molecules (Basel, Switzerland) · 2023Review
- Dynamic changes in whole genome DNA methylation, chromatin and gene expression during mouse lens differentiation.Epigenetics & chromatin · 2023Article
- Molecular basis of hUHRF1 allosteric activation for synergistic histone modification binding by PI5P.Science advances · 2022Article
- The dCypher Approach to Interrogate Chromatin Reader Activity Against Posttranslational Modification-Defined Histone Peptides and Nucleosomes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Comprehensive Pan-Cancer Analysis Reveals the Role of UHRF1-Mediated DNA Methylation and Immune Infiltration in Renal Cell Carcinoma.Journal of oncology · 2022Article
- TIP60 governs the auto‑ubiquitination of UHRF1 through USP7 dissociation from the UHRF1/USP7 complex.International journal of oncology · 2021Article
- The multi-functionality of UHRF1: epigenome maintenance and preservation of genome integrity.Nucleic acids research · 2021Review
- Discovery of small molecules targeting the tandem tudor domain of the epigenetic factor UHRF1 using fragment-based ligand discovery.Scientific reports · 2021Article
- In silico APC/C substrate discovery reveals cell cycle-dependent degradation of UHRF1 and other chromatin regulators.PLoS biology · 2020Article
- Alternative splicing and allosteric regulation modulate the chromatin binding of UHRF1.Nucleic acids research · 2020Article
- A critical role of PRDM14 in human primordial germ cell fate revealed by inducible degrons.Nature communications · 2020Article
- Epigenetic factors Dnmt1 and Uhrf1 coordinate intestinal development.Developmental biology · 2019Article
- UHRF1 promotes renal cell carcinoma progression through epigenetic regulation of TXNIP.Oncogene · 2019Article
- Nuclear Phosphoinositides: Their Regulation and Roles in Nuclear Functions.International journal of molecular sciences · 2019Review
- Coordinated Dialogue between UHRF1 and DNMT1 to Ensure Faithful Inheritance of Methylated DNA Patterns.Genes · 2019Review
- Targeting the SET and RING-associated (SRA) domain of ubiquitin-like, PHD and ring finger-containing 1 (UHRF1) for anti-cancer drug development.Oncotarget · 2018Review
- Conformational dynamics of the TTD-PHD histone reader module of the UHRF1 epigenetic regulator reveals multiple histone-binding states, allosteric regulation, and druggability.The Journal of biological chemistry · 2017Article
- A histone-mimicking interdomain linker in a multidomain protein modulates multivalent histone binding.The Journal of biological chemistry · 2017Article
- Article
- Gender Differences in Global but Not Targeted Demethylation in iPSC Reprogramming.Cell reports · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin-like with PHD and RING Finger domains 1 (UHRF1) is an important nuclear protein that is mutated and aberrantly expressed in many tumors. The protein integrates different chromatin modifications and is essential for their maintenance throughout the cell cycle. Separate chromatin-binding modules of UHRF1 have been studied on a functional and structural level. The unmodified N-terminus of histone H3 is recognized by a PHD domain, while a TTD domain specifically interacts with histone H3 Lysine 9 trimethylation. A SRA region binds hemimethylatd DNA. Emerging evidence indicates that the modules of UHRF1 do not act independently of each other but establish complex modes of interaction with patterns of chromatin modifications. This multivalent readout is regulated by allosteric binding of phosphatidylinositol 5-phosphate to a region outside the PHD, TTD and SRA domains as well as by phosphorylation of one of the linker regions connecting these modules. Here, we summarize the current knowledge on UHRF1 chromatin interaction and introduce a novel model of conformational transitions of the protein that are directed by the flexible and highly charged linker regions. We propose that these are essential in setting up defined structural states of the protein where different domains or combinations thereof are available for binding chromatin modifications or are prevented from doing so. Lastly, we suggest that controlled tuning of intramolecular linker interactions by ligands and posttranslational modifications establishes a rational framework for comprehending UHRF1 regulation and putatively the working mode of other chromatin factors in different physiological contexts.
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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.