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J. Exp. Med., Volume 189, Number 8, April 19, 1999 1181-1194

SHP2-interacting Transmembrane Adaptor Protein (SIT), A Novel Disulfide-linked Dimer Regulating Human T Cell Activation

By Anne Marie-Cardine,* Henning Kirchgessner,* Eddy Bruyns,* Andrej Shevchenko,§ Matthias Mann,§ Frank Autschbach,Dagger Sheldon Ratnofsky,parallel Stefan Meuer,* and Burkhart Schraven*

From the * Immunomodulation Laboratory of the Institute for Immunology, and the Dagger  Institute for Pathology, University of Heidelberg, 69120 Heidelberg, Germany; the § Protein and Peptide Group, European Molecular Biology Laboratories, 69117 Heidelberg, Germany; and the parallel  BASF Bioresearch Corporation, Worcester, Massachusetts 01605

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.

Key words: T lymphocytes;  T cell receptor;  transmembrane adaptor proteins;  signal transduction


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