The Journal of Experimental Medicine
CSHL 2010 Immunology Conference
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© The Rockefeller University Press, 0022-1007/1998/8/561/ $5.00
The Journal of Experimental Medicine, Volume 188, Number 3, August 3, 1998 561-575

Articles

T Cell Receptor (TCR) Interacting Molecule (TRIM), A Novel Disulfide-linked Dimer Associated with the TCR–CD3–{zeta} Complex, Recruits Intracellular Signaling Proteins to the Plasma Membrane

Eddy Bruyns*, Anne Marie-Cardine*, Henning Kirchgessner*, Karin Sagolla*, Andrej Shevchenko§, Matthias Mann§, Frank Autschbach{ddagger}, Armand Bensussan||, Stefan Meuer*, and Burkhart Schraven*

From the * Institute for Immunology and the {ddagger} Institute for Pathology, University of Heidelberg, 69120 Heidelberg, Germany; the § Protein and Peptide Group, European Molecular Biology Laboratories, 69117 Heidelberg, Germany; and the || Faculté de Médecine de Créteil, INSERM U448, 94010 Créteil Cedex, France

The molecular mechanisms regulating recruitment of intracellular signaling proteins like growth factor receptor–bound protein 2 (Grb2), phospholipase C{gamma}1, or phosphatidylinositol 3-kinase (PI3-kinase) to the plasma membrane after stimulation of the T cell receptor (TCR)– CD3–{zeta} complex are not very well understood. We describe here purification, tandem mass spectrometry sequencing, molecular cloning, and biochemical characterization of a novel transmembrane adaptor protein which associates and comodulates with the TCR–CD3–{zeta} complex in human T lymphocytes and T cell lines. This protein was termed T cell receptor interacting molecule (TRIM). TRIM is a disulfide-linked homodimer which is comprised of a short extracellular domain of 8 amino acids, a 19–amino acid transmembrane region, and a 159–amino acid cytoplasmic tail. In its intracellular domain, TRIM contains several tyrosine-based signaling motifs that could be involved in SH2 domain–mediated protein–protein interactions. Indeed, after T cell activation, TRIM becomes rapidly phosphorylated on tyrosine residues and then associates with the 85-kD regulatory subunit of PI3-kinase via an YxxM motif. Thus, TRIM represents a TCR-associated transmembrane adaptor protein which is likely involved in targeting of intracellular signaling proteins to the plasma membrane after triggering of the TCR.

Key Words: T lymphocytes • T cell receptor • transmembrane adaptor proteins

Address correspondence to Burkhart Schraven, Institute for Immunology, Immunomodulation Laboratory, University of Heidelberg, Im Neuenheimer Feld 305, 69120 Heidelberg, Germany. Phone: 49-6221-56-4059; Fax: 49-6221-56-5541; E-mail: m53{at}popix.urz.uni-heidelberg.de

A. Marie-Cardine is a recipient of a fellowship from the Training and Mobility of Researchers program of the European Community (ERBFMBICT950472). This work was supported in part by the Deutsche Forschungs Gemeinschaft grants SCHR/533/1-1 and SFB 405/A5 (B. Schraven) and B9 (F. Autschbach). The work in M. Mann's laboratory was supported in part by a generous grant from the German Technology Ministry (BMBF).

M. Mann's present address is Center of Experimental Bioinformatics, Odense University, Staermosegaadsvej 16, DK-5230 Odense M, Denmark.

E. Bruyns, A. Marie-Cardine, and H. Kirchgessner contributed equally to this work.

Abbreviations used: Grb2, growth factor receptor–bound protein 2; GST, glutathione-S-transferase; IEF, isoelectric focussing; LAT, linker for activation of T cells; MAP, mitogen-activated protein; PI3-kinase, phosphatidylinositol 3-kinase; PTK, protein tyrosine kinase; PTYR, phosphotyrosine; RACE, rapid amplification of cDNA ends; SH2, src homology 2; SKAP55, src kinase–associated phosphoprotein of 55 kD; TRIM, T cell receptor interacting molecule(s).


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