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



From the * Department for Molecular Immunology, Biology III, University of Freiburg, 79104 Freiburg, Germany; and the The B cell antigen receptor (BCR) consists of the membrane-bound immunoglobulin (Ig)
molecule as antigen-binding subunit and the Ig-
Max-Planck-Institute for Immunobiology, 79108 Freiburg, Germany
/Ig-
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.
This article has been cited by other articles:
| TABLE OF CONTENTS |
|