Association of SLP-65 / BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-α
Authors:
- 1 July 2001
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 31 (7) , 2126-2134
Abstract
The cytoplasmic adaptor protein SLP-65 (BLNK or BASH) is a cricital downstream effector of the B cell antigen receptor (BCR). Tyrosine-phosphorylated SLP-65 assembles intracellular signaling complexes such as the Ca2 + initiation complex encompassing phospholipase C-γ2 and Bruton′s tyrosine kinase. It is, however, unclear how the SLP-65 signaling module can be recruited to the plasma membrane. Here we show that following B cell stimulation, SLP-65 associates directly with the BCR signaling subunit, the Ig-α / Ig-β heterodimer. The interaction is mediated by theSrc homology 2 domain of SLP-65 and the phosphorylated Ig-α tyrosine 204, which is located outside of the immunoreceptor tyrosine-based activation motif. Our data identify an unexpected BCR phosphorylation pattern and indicate that Ig-α has the capability to serve as transmembrane adaptor in BCR signaling.Keywords
This publication has 53 references indexed in Scilit:
- B Cell Development Is Arrested at the Immature B Cell Stage in Mice Carrying a Mutation in the Cytoplasmic Domain of Immunoglobulin βJournal of Experimental Medicine, 2000
- Intracellular adapter moleculesSeminars in Immunology, 2000
- Ig-α Cytoplasmic Truncation Renders Immature B Cells More Sensitive to Antigen ContactImmunity, 1999
- A Negative Regulatory Role for Ig-α during B Cell DevelopmentImmunity, 1999
- Structural basis for syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptideJournal of Molecular Biology, 1998
- BLNKImmunity, 1998
- The Immunoglobulin (Ig)α and Igβ Cytoplasmic Domains Are Independently Sufficient to Signal B Cell Maturation and Activation in Transgenic MiceJournal of Experimental Medicine, 1997
- The cytoplasmic domains of immunoglobulin (Ig) alpha and Ig beta can independently induce the precursor B cell transition and allelic exclusion.Journal of Experimental Medicine, 1995
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and FynCurrent Biology, 1993