ArticleMolecular and cellular biology2003
The cyclin E/Cdk2 substrate and Cajal body component p220(NPAT) activates histone transcription through a novel LisH-like domain.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 82 citations in OpenAlex.
- Cell-cycle-dependent repression of histone gene transcription by histone H4.Nature structural & molecular biology · 2026Article
- Nuclear ribonucleoprotein condensates as platforms for gene expression regulation.Genes & genomics · 2025Review
- Cell-cycle-regulated transcriptional pausing ofMolecular biology of the cell · 2025Article
- KPNA3 regulates histone locus body formation by modulating condensation and nuclear import of NPAT.The Journal of cell biology · 2025Article
- Cell cycle-regulated transcriptional pausing ofbioRxiv : the preprint server for biology · 2024Article
- Histone locus bodies: a paradigm for how nuclear biomolecular condensates control cell cycle regulated gene expression.Nucleus (Austin, Tex.) · 2023Review
- Coordinated expression of replication-dependent histone genes from multiple loci promotes histone homeostasis inMolecular biology of the cell · 2023Article
- Cell cycle regulators and bone: development and regeneration.Cell & bioscience · 2023Review
- Mxc, a Drosophila homolog of mental retardation-associated gene NPAT, maintains neural stem cell fate.Cell & bioscience · 2022Article
- Superresolution light microscopy of theMolecular biology of the cell · 2021Article
- CDK-Regulated Phase Separation Seeded by Histone Genes Ensures Precise Growth and Function of Histone Locus Bodies.Developmental cell · 2020Article
- Article
- Hsp70 Interacts with Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinase 2 To Regulate p38MAPK Stability and Myoblast Differentiation during Skeletal Muscle Regeneration.Molecular and cellular biology · 2018Article
- Regulation of DNA replication-coupled histone gene expression.Oncotarget · 2017Review
- Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017Review
- Histone locus regulation by theGenes & development · 2017Article
- Coordinating cell cycle-regulated histone gene expression through assembly and function of the Histone Locus Body.RNA biology · 2017Review
- Proteomic Landscape of Tissue-Specific Cyclin E Functions in Vivo.PLoS genetics · 2016Article
- Localization and interactions of Plasmodium falciparum SWIB/MDM2 homologues.Malaria journal · 2016Article
- Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2 Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved in Regulating Histone Transcription.The Journal of biological chemistry · 2015Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
p220(NPAT) is a substrate of cyclin E/Cdk2 that localizes in nuclear organelles called Cajal bodies in a cell cycle-regulated manner. In normal diploid fibroblasts, p220 is concentrated in two Cajal bodies tethered to histone gene clusters at chromosome 6p21 during G(1), S, and G(2) phases and two additional Cajal bodies tethered to histone genes at 1q21 during S, and G(2) phases. Overexpression of p220 in U2OS cells can promote the G(1)/S transition and can also promote transcription from histone H2B and H4 luciferase reporter constructs. How p220 expression induces these activities and whether the two activities are related are unknown. In this study, we developed a "lox-scanning" mutagenesis approach to identify functional domains in p220. We identified two distinct functional regions of p220. The C-terminal half of the protein contains multiple elements that are required for its ability to induce S phase in transfected cells. In contrast, sequences at the N terminus appear to be critical for activation of histone H4 and H2B reporter constructs. We identified an approximately 30-amino-acid motif at the N terminus of p220 that has the characteristics of a LisH motif. LisH motifs are found in a large number of proteins in the database but are of unknown function. Point mutations in conserved residues in the LisH motif of p220 block histone H4 transcriptional activity without affecting localization in Cajal bodies or phosphorylation on Cdk2 phosphorylation sites. These studies indicate that the ability of p220 to promote S phase is independent of its ability to promote histone H4 transcription and suggests that p220 may link cyclin E/Cdk2 to multiple independent downstream functions.
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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.