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Oncogenic kinase signalling

Author

Listed:
  • Peter Blume-Jensen

    (The Salk Institute, Molecular and Cell Biology Laboratory
    Serono Reproductive Biology Institute)

  • Tony Hunter

    (The Salk Institute, Molecular and Cell Biology Laboratory
    Serono Reproductive Biology Institute)

Abstract

Protein-tyrosine kinases (PTKs) are important regulators of intracellular signal-transduction pathways mediating development and multicellular communication in metazoans. Their activity is normally tightly controlled and regulated. Perturbation of PTK signalling by mutations and other genetic alterations results in deregulated kinase activity and malignant transformation. The lipid kinase phosphoinositide 3-OH kinase (PI(3)K) and some of its downstream targets, such as the protein-serine/threonine kinases Akt and p70 S6 kinase (p70S6K), are crucial effectors in oncogenic PTK signalling. This review emphasizes how oncogenic conversion of protein kinases results from perturbation of the normal autoinhibitory constraints on kinase activity and provides an update on our knowledge about the role of deregulated PI(3)K/Akt and mammalian target of rapamycin/p70S6K signalling in human malignancies.

Suggested Citation

  • Peter Blume-Jensen & Tony Hunter, 2001. "Oncogenic kinase signalling," Nature, Nature, vol. 411(6835), pages 355-365, May.
    • Handle: RePEc:nat:nature:v:411:y:2001:i:6835:d:10.1038_35077225
    DOI: 10.1038/35077225
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    Cited by:

    1. Jeongah Yoon & Thomas S Deisboeck, 2009. "Investigating Differential Dynamics of the MAPK Signaling Cascade Using a Multi-Parametric Global Sensitivity Analysis," PLOS ONE, Public Library of Science, vol. 4(2), pages 1-14, February.
    2. Gianna Maria Nardi & Elisabetta Ferrara & Ilaria Converti & Francesca Cesarano & Salvatore Scacco & Roberta Grassi & Antonio Gnoni & Felice Roberto Grassi & Biagio Rapone, 2020. "Does Diabetes Induce the Vascular Endothelial Growth Factor (VEGF) Expression in Periodontal Tissues? A Systematic Review," IJERPH, MDPI, vol. 17(8), pages 1-16, April.
    3. Sichun Yang & Benoît Roux, 2008. "Src Kinase Conformational Activation: Thermodynamics, Pathways, and Mechanisms," PLOS Computational Biology, Public Library of Science, vol. 4(3), pages 1-14, March.
    4. Kousik Kundu & Fabrizio Costa & Michael Huber & Michael Reth & Rolf Backofen, 2013. "Semi-Supervised Prediction of SH2-Peptide Interactions from Imbalanced High-Throughput Data," PLOS ONE, Public Library of Science, vol. 8(5), pages 1-15, May.
    5. Hipólito Nicolás Cuesta-Hernández & Julia Contreras & Pablo Soriano-Maldonado & Jana Sánchez-Wandelmer & Wayland Yeung & Ana Martín-Hurtado & Inés G. Muñoz & Natarajan Kannan & Marta Llimargas & Javie, 2023. "An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function," Nature Communications, Nature, vol. 14(1), pages 1-21, December.
    6. Hui-Rong Xu & Zhong-Fa Xu & Yan-Lai Sun & Jian-Jun Han & Zeng-Jun Li, 2013. "The −842G/C Polymorphisms of PIN1 Contributes to Cancer Risk: A Meta-Analysis of 10 Case-Control Studies," PLOS ONE, Public Library of Science, vol. 8(8), pages 1-7, August.
    7. Martin Klammer & J Nikolaj Dybowski & Daniel Hoffmann & Christoph Schaab, 2015. "Pareto Optimization Identifies Diverse Set of Phosphorylation Signatures Predicting Response to Treatment with Dasatinib," PLOS ONE, Public Library of Science, vol. 10(6), pages 1-16, June.
    8. Zhongtao Zhao & Qiaojun Jin & Jin-Rong Xu & Huiquan Liu, 2014. "Identification of a Fungi-Specific Lineage of Protein Kinases Closely Related to Tyrosine Kinases," PLOS ONE, Public Library of Science, vol. 9(2), pages 1-8, February.
    9. Qiwei Jiang & Xiaomei Zhang & Xiaoming Dai & Shiyao Han & Xueji Wu & Lei Wang & Wenyi Wei & Ning Zhang & Wei Xie & Jianping Guo, 2022. "S6K1-mediated phosphorylation of PDK1 impairs AKT kinase activity and oncogenic functions," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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