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. Author manuscript; available in PMC: 2014 Oct 1.
Published in final edited form as: Nat Immunol. 2014 Mar 2;15(4):384–392. doi: 10.1038/ni.2843

Figure 3.

Figure 3

Protein-protein interactions within the Zap70–Lat–SLP-76 interaction network of mouse CD4+ T cells. Bait proteins corresponded to the Zap70, Lat and SLP-76 proteins. Protein-protein interactions were identified by affinity purification and mass-spectrometry prior to and at 30, 120 and 300 s after stimulation and visualized using Cystoscape v.2.8.3. Several proteins were found associated with more than one bait (“shared interactome”). Zap-70 was the only tested bait capable of capturing the subunits of the TCR-CD3 complex (blue box). Node functions were assigned according to the legend shown in the top left corner and encompass transmembrane receptor, tyrosine or serine/threonine protein kinase (Kinase), phospholipid or tyrosine protein phosphatase (Phosphatase), guanine exchange factor (GEF), GTP-ase activating protein (GAP), ion channel, transporter, ubiquitin ligase (E3 ligase). The depicted interactions have been observed in at least two out of three independent experiments involving three biological replicates each. Each of the proteins is denoted by its Uniprot symbol (see Supplementary Table 1) except LCP2 that is called SLP-76. For more details on identified high confidence network components and protein interaction see also Supplementary Tables 1,2.