The Dok-3/Grb2 Protein Signal Module Attenuates Lyn Kinase-dependent Activation of Syk Kinase in B Cell Antigen Receptor Microclusters
2013 | journal article. A publication with affiliation to the University of Göttingen.
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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
Loesing, M.; Goldbeck, I.; Manno, B.; Oellerich, T.; Schnyder, T.; Bohnenberger, H. & Stork, B. et al. (2013)
Journal of Biological Chemistry, 288(4) pp. 2303-2313. DOI: https://doi.org/10.1074/jbc.M112.406546
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Details
- Authors
- Loesing, Marion; Goldbeck, Ingo; Manno, Birgit; Oellerich, Thomas; Schnyder, Tim; Bohnenberger, Hanibal; Stork, Bjoern; Urlaub, Henning; Batista, Facundo D.; Wienands, Juergen ; Engelke, Michael
- Abstract
- 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.
- Issue Date
- 2013
- Status
- published
- Publisher
- Amer Soc Biochemistry Molecular Biology Inc
- Journal
- Journal of Biological Chemistry
- ISSN
- 0021-9258