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J. Exp. Med.,
Volume 189, Number 8, April 19, 1999 1181-1194
By
From the * Immunomodulation Laboratory of the Institute for Immunology, and the T lymphocytes express several low molecular weight transmembrane adaptor proteins that recruit src homology (SH)2 domain-containing intracellular molecules to the cell membrane via
tyrosine-based signaling motifs. We describe here a novel molecule of this group termed SIT
(SHP2 interacting transmembrane adaptor protein). SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes. After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase
SHP2 via an immunoreceptor tyrosine-based inhibition motif. Overexpression of SIT in Jurkat
cells downmodulates T cell receptor- and phytohemagglutinin-mediated activation of the nuclear factor of activated T cells (NF-AT) by interfering with signaling processes that are probably located upstream of activation of phospholipase C. However, binding of SHP2 to SIT is
not required for inhibition of NF-AT induction, suggesting that SIT not only regulates NF-AT
activity but also controls NF-AT unrelated pathways of T cell activation involving SHP2.
Institute for
Pathology, University of Heidelberg, 69120 Heidelberg, Germany; the § Protein and Peptide Group,
European Molecular Biology Laboratories, 69117 Heidelberg, Germany; and the BASF Bioresearch
Corporation, Worcester, Massachusetts 01605
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