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J. Exp. Med., Volume 188, Number 4, August 17, 1998 791-795

SLP-65: A New Signaling Component in B Lymphocytes which Requires Expression of the Antigen Receptor for Phosphorylation

By Jürgen Wienands,* Jutta Schweikert,* Bernd Wollscheid,* Hassan Jumaa,Dagger Peter J. Nielsen,Dagger and Michael Reth*Dagger

From the * Department for Molecular Immunology, Biology III, University of Freiburg, 79104 Freiburg, Germany; and the Dagger  Max-Planck-Institute for Immunobiology, 79108 Freiburg, Germany

The B cell antigen receptor (BCR) consists of the membrane-bound immunoglobulin (Ig) molecule as antigen-binding subunit and the Ig-alpha /Ig-beta heterodimer as signaling subunit. BCR signal transduction involves activation of protein tyrosine kinases (PTKs) and phosphorylation of several proteins, only some of which have been identified. The phosphorylation of these proteins can be induced by exposure of B cells either to antigen or to the tyrosine phosphatase inhibitor pervanadate/H2O2. One of the earliest substrates in B cells is a 65-kD protein, which we identify here as a B cell adaptor protein. This protein, named SLP-65, is part of a signaling complex involving Grb-2 and Vav and shows homology to SLP-76, a signaling element of the T cell receptor. In pervanadate/H2O2-stimulated cells, SLP-65 becomes phosphorylated only upon expression of the BCR. These data suggest that SLP-65 is part of a BCR transducer complex.

Key words: antigen receptortyrosine phosphorylationSrc homology 2 domainSLP-65


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