ArticleThe EMBO journal2002
Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 65 citations in OpenAlex.
- Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- TTT (Tel2-Tti1-Tti2) Complex, the Co-Chaperone of PIKKs and a Potential Target for Cancer Chemotherapy.International journal of molecular sciences · 2023Review
- CK2 and the Hallmarks of Cancer.Biomedicines · 2022Review
- Copper Modulates the Catalytic Activity of Protein Kinase CK2.Frontiers in molecular biosciences · 2022Article
- CK2 Regulation: Perspectives in 2021.Biomedicines · 2021Review
- FGF1 induces resistance to chemotherapy in ovarian granulosa tumor cells through regulation of p53 mitochondrial localization.Oncogenesis · 2018Article
- Identification of new FGF1 binding partners-Implications for its intracellular function.IUBMB life · 2016Article
- Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity.Cellular and molecular life sciences : CMLS · 2015Review
- Nucleolin regulates phosphorylation and nuclear export of fibroblast growth factor 1 (FGF1).PloS one · 2014Article
- Functional roles of fibroblast growth factor receptors (FGFRs) signaling in human cancers.Apoptosis : an international journal on programmed cell death · 2013Review
- Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration.Scientific reports · 2012Article
- Fibroblast growth factor-12 (FGF12) translocation into intestinal epithelial cells is dependent on a novel cell-penetrating peptide domain: involvement of internalization in the in vivo role of exogenous FGF12.The Journal of biological chemistry · 2011Article
- Ability of CK2beta to selectively regulate cellular protein kinases.Molecular and cellular biochemistry · 2008Article
- Protein kinase CK2, an important regulator of the inflammatory response?Journal of molecular medicine (Berlin, Germany) · 2008Review
- Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus.Molecular and cellular biology · 2008Article
- Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1.Molecular biology of the cell · 2005Article
- Translocation of FGF-1 and FGF-2 across vesicular membranes occurs during G1-phase by a common mechanism.Molecular biology of the cell · 2004Article
- Nuclear localization and function of polypeptide ligands and their receptors: a new paradigm for hormone specificity within the mammary gland?Breast cancer research : BCR · 2003Review
- Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.The Biochemical journal · 2003Review
- Vesicle transmembrane potential is required for translocation to the cytosol of externally added FGF-1.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast growth factor-1 (FGF-1) has both extra- and intracellular functions. To identify intracellular binding partners for FGF-1, we isolated proteins from U2OS human osteosarcoma cells interacting specifically with FGF-1. One of the isolated proteins was identified as protein kinase CK2 (CK2). We here provide evidence that FGF-1 binds to both the catalytic alpha-subunit and to the regulatory beta-subunit of CK2. The interaction between FGF-1 and CK2 alpha and beta was characterized by surface plasmon resonance, giving K(D) values of 0.4 +/- 0.3 and 1.2 +/- 0.2 microM, respectively. By using a novel assay for intracellular protein interaction, FGF-1 and CK2 alpha are shown to interact in vivo. In vitro, FGF-1 and FGF-2 are phosphorylated by CK2, and the presence of FGF-1 or FGF-2 was found to enhance the autophosphorylation of CK2 beta. A correlation between the mitogenic potential of FGF-1 mutants and their ability to bind to CK2 alpha was observed. The possible involvement of CK2 in the FGF-induced stimulation of DNA synthesis is discussed.
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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.