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The Dok-3/Grb2 protein signal module attenuates Lyn kinase-dependent activation of Syk kinase in B cell antigen receptor microclusters.

MPG-Autoren
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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://www.jbc.org/content/288/4/2303.full.pdf+html?sid=a6b75591-ef19-4cdc-ac40-b86c2962b516
(Verlagsversion)

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Zitation

Lösing, M., Goldbeck, I., Manno, B., Oellerich, T., Schnyder, T., Bohnenberger, H., et al. (2013). The Dok-3/Grb2 protein signal module attenuates Lyn kinase-dependent activation of Syk kinase in B cell antigen receptor microclusters. Journal of Biological Chemistry, 288(4), 2303-2313. doi:10.1074/jbc.M112.406546.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000E-ECF6-8
Zusammenfassung
Recruitment of the growth factor receptor-bound protein 2 (Grb2) by the plasma membrane-associated adapter protein downstream of kinase 3 (Dok-3) attenuates signals transduced by the B cell antigen receptor (BCR). Here we describe molecular details of Dok-3/Grb2 signal integration and function, showing that the Lyn-dependent activation of the BCR transducer kinase Syk is attenuated by Dok-3/Grb2 in a site-specific manner. This process is associated with the SH3 domain-dependent translocation of Dok-3/Grb2 complexes into BCR microsignalosomes and augmented phosphorylation of the inhibitory Lyn target SH2 domain-containing inositol 5′ phosphatase. Hence, our findings imply that Dok-3/Grb2 modulates the balance between activatory and inhibitory Lyn functions with the aim to adjust BCR signaling efficiency.