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. 2008 Mar 1;94(5):1766–1772. doi: 10.1529/biophysj.107.116590

Figure 1.

Figure 1

(A) Schematic representation of GADS-related signaling in T cells. TCR ligation induces side-specific phosphorylation of the intracellular chains of the TCR/CD3 complex. These initial events trigger phosphorylation of LAT and SLP-76. SLP-76 is subsequently recruited to LAT via GADS. This trimolecular complex (LAT/GADS/SLP-76) then recruits other modular proteins (VAV, NCK, ADAP, ITK, GAB2, PLCγ). The formation of this complex is required for the activation of the RAS-MAPK pathway and for the cytoskeleton reorganization. (B) Schematic representation of full-length GADS. GADS is composed of SH3-SH2 domains at the N-terminus and a C-terminal SH3 domain. These are separated by a long unstructured region composed of 126 amino acid residues. The SH2 domain of GADS binds phosphorylated LAT; the C-terminal SH3 domain binds the adaptor molecule SLP-76; the binding partner and the functional role of the N-terminal SH3 domain are still unknown.