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Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases

Author

Listed:
  • Masahiro Kawabuchi

    (Divisions of Protein Metabolism)

  • Yoshinori Satomi

    (Organic Chemistry, Institute for Protein Research, Osaka University)

  • Toshifumi Takao

    (Organic Chemistry, Institute for Protein Research, Osaka University)

  • Yasutsugu Shimonishi

    (Organic Chemistry, Institute for Protein Research, Osaka University)

  • Shigeyuki Nada

    (Institute of Scientific and Industrial Research Osaka University)

  • Katsuya Nagai

    (Divisions of Protein Metabolism)

  • Alexander Tarakhovsky

    (Laboratory for Lymphocyte Signalling, Institute for Genetics, University of Cologne)

  • Masato Okada

    (Divisions of Protein Metabolism)

Abstract

The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk, which specifically phosphorylates a conserved regulatory tyrosine residue at the carboxy-terminal tail of the Src-PTKs1,2,3. Csk is mainly cytoplasmic and Src-PTKs are predominantly membrane-associated. This raises a question about the mechanism of interaction between these enzymes. Here we present Cbp—a transmembrane phosphoprotein that is ubiquitously expressed and binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in the Csk-mediated inhibition of c-Src. In the plasma membrane Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signalling4,5,6,7,8. These findings reveal Cbp as a new component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.

Suggested Citation

  • Masahiro Kawabuchi & Yoshinori Satomi & Toshifumi Takao & Yasutsugu Shimonishi & Shigeyuki Nada & Katsuya Nagai & Alexander Tarakhovsky & Masato Okada, 2000. "Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases," Nature, Nature, vol. 404(6781), pages 999-1003, April.
    • Handle: RePEc:nat:nature:v:404:y:2000:i:6781:d:10.1038_35010121
    DOI: 10.1038/35010121
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    Cited by:

    1. Michael A Jamros & Leandro C Oliveira & Paul C Whitford & José N Onuchic & Joseph A Adams & Patricia A Jennings, 2012. "Substrate-Specific Reorganization of the Conformational Ensemble of CSK Implicates Novel Modes of Kinase Function," PLOS Computational Biology, Public Library of Science, vol. 8(9), pages 1-8, September.
    2. Dhivya Sridaran & Surbhi Chouhan & Kiran Mahajan & Arun Renganathan & Cody Weimholt & Shambhavi Bhagwat & Melissa Reimers & Eric H. Kim & Manish K. Thakur & Muhammad A. Saeed & Russell K. Pachynski & , 2022. "Inhibiting ACK1-mediated phosphorylation of C-terminal Src kinase counteracts prostate cancer immune checkpoint blockade resistance," Nature Communications, Nature, vol. 13(1), pages 1-21, December.

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