ArticleThe Journal of biological chemistry2011
Hierarchical phosphorylation within the ankyrin repeat domain defines a phosphoregulatory loop that regulates Notch transcriptional activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 45 citations in OpenAlex.
- The role of ankyrin repeat-containing proteins in epigenetic and transcriptional regulation.Cell death discovery · 2025Review
- Regulation of Notch1 Signalling by Long Non-Coding RNAs in Cancers and Other Health Disorders.International journal of molecular sciences · 2023Review
- CK2 and the Hallmarks of Cancer.Biomedicines · 2022Review
- Sirtuin1 meditated modification of Notch1 intracellular domain regulates nucleolar localization and activation of distinct signaling cascades.Frontiers in cell and developmental biology · 2022Article
- CK2β-regulated signaling controls B cell differentiation and function.Frontiers in immunology · 2022Article
- Protein Kinase CK2 Regulates B Cell Development and Differentiation.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Pharmacological Disruption of the Notch1 Transcriptional Complex Inhibits Tumor Growth by Selectively Targeting Cancer Stem Cells.Cancer research · 2021Article
- CDK5 positively regulates Notch1 signaling in pancreatic cancer cells by phosphorylation.Cancer medicine · 2021Article
- To Divide or Invade: A Look Behind the Scenes of the Proliferation-Invasion Interplay in theFrontiers in cell and developmental biology · 2020Review
- Making sense out of missense mutations: Mechanistic dissection of Notch receptors through structure-function studies in Drosophila.Development, growth & differentiation · 2020Review
- Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Extension of the Notch intracellular domain ankyrin repeat stack by NRARP promotes feedback inhibition of Notch signaling.Science signaling · 2019Article
- The nuclear pore proteins Nup88/214 and T-cell acute lymphatic leukemia-associated NUP214 fusion proteins regulate Notch signaling.The Journal of biological chemistry · 2019Article
- C-terminal deletion of NOTCH1 intracellular domain (N1Scientific reports · 2017Article
- The Varied Roles of Notch in Cancer.Annual review of pathology · 2017Review
- CK2 inhibitor CX-4945 destabilizes NOTCH1 and synergizes with JQ1 against human T-acute lymphoblastic leukemic cells.Haematologica · 2017Article
- Non-epigenetic function of HDAC8 in regulating breast cancer stem cells by maintaining Notch1 protein stability.Oncotarget · 2016Article
- Notch Signaling in Neuroendocrine Tumors.Frontiers in oncology · 2016Review
- Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity.Cellular and molecular life sciences : CMLS · 2015Review
- Phosphorylation-dependent regulation of Notch1 signaling: the fulcrum of Notch1 signaling.BMB reports · 2015Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The Notch signal transduction pathway mediates important cellular functions through direct cell-to-cell contact. Deregulation of Notch activity can lead to an altered cell proliferation and has been linked to many human cancers. Casein kinase 2 (CK2), a ubiquitous kinase, regulates several cellular processes by phosphorylating proteins involved in signal transduction, gene expression, and protein synthesis. In this report we identify Notch(ICD) as a novel target of phosphorylation by CK2. Using mapping and mutational studies, we identified serine 1901, located in the ankyrin domain of Notch, as the target amino acid. Interestingly, phosphorylation of serine 1901 by CK2 appears to generate a second phosphorylation site at threonine 1898. Furthermore, threonine 1898 phosphorylation only occurs when Notch forms a complex with Mastermind and CSL. Phosphorylation of both threonine 1898 and serine 1901 resulted in decreased binding of the Notch-Mastermind-CSL ternary complex to DNA and consequently lower transcriptional activity. These data indicate that the phosphorylation of serine 1901 and threonine 1898 negatively regulates Notch function by dissociating the complex from DNA. This study identifies a new component involved in regulation of Notch(ICD) transcriptional activity, reinforcing the notion that a precise and tight regulation is required for this essential signaling pathway.
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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.