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Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads.

Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE, Mariuzza RA
EMBO J 23 1441-51 (2004)
Related entries: 1r1q, 1r1s

Cited: 24 times
EuropePMC logo PMID: 15029250

Abstract

The transmembrane protein, linker for activation of T cells (LAT), is essential for T-cell activation and development. Phosphorylation of LAT at multiple tyrosines creates binding sites for the adaptors Gads and Grb2, leading to nucleation of multiprotein signaling complexes. Human LAT contains five potential binding sites for Gads, of which only those at Tyr171 and Tyr191 appear necessary for T-cell function. We asked whether Gads binds preferentially to these sites, as differential recognition could assist in assembling defined LAT-based complexes. Measured calorimetrically, Gads-SH2 binds LAT tyrosine phosphorylation sites 171 and 191 with higher affinities than the other sites, with the differences ranging from only several fold weaker binding to no detectable interaction. Crystal structures of Gads-SH2 complexed with phosphopeptides representing sites 171, 191 and 226 were determined to 1.8-1.9 A resolutions. The structures reveal the basis for preferential recognition of specific LAT sites by Gads, as well as for the relatively greater promiscuity of the related adaptor Grb2, whose binding also requires asparagine at position +2 C-terminal to the phosphorylated tyrosine.

Reviews - 1r1p mentioned but not cited (1)

  1. Bridging the Gap: Modulatory Roles of the Grb2-Family Adaptor, Gads, in Cellular and Allergic Immune Responses. Yablonski D. Front Immunol 10 1704 (2019)

Articles - 1r1p mentioned but not cited (2)

  1. Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads. Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE, Mariuzza RA. EMBO J. 23 1441-1451 (2004)
  2. Configuration Synthesis and Performance Analysis of Finger Soft Actuator. Zhang Z, Chen H, Zhang Z. Appl Bionics Biomech 2018 4264560 (2018)


Reviews citing this publication (4)

  1. Experimental detection of short regulatory motifs in eukaryotic proteins: tips for good practice as well as for bad. Gibson TJ, Dinkel H, Van Roey K, Diella F. Cell Commun. Signal 13 42 (2015)
  2. An Interaction Library for the FcεRI Signaling Network. Chylek LA, Holowka DA, Baird BA, Hlavacek WS. Front Immunol 5 172 (2014)
  3. How the Discovery of the CD4/CD8-p56lck Complexes Changed Immunology and Immunotherapy. Rudd CE. Front Cell Dev Biol 9 626095 (2021)
  4. Structural conservation of a short, functional, peptide-sequence motif. Fox-Erlich S, Schiller MR, Gryk MR. Front Biosci (Landmark Ed) 14 1143-1151 (2009)

Articles citing this publication (17)

  1. Persistence of cooperatively stabilized signaling clusters drives T-cell activation. Bunnell SC, Singer AL, Hong DI, Jacque BH, Jordan MS, Seminario MC, Barr VA, Koretzky GA, Samelson LE. Mol. Cell. Biol. 26 7155-7166 (2006)
  2. Aggregation of membrane proteins by cytosolic cross-linkers: theory and simulation of the LAT-Grb2-SOS1 system. Nag A, Monine MI, Faeder JR, Goldstein B. Biophys. J. 96 2604-2623 (2009)
  3. Loops govern SH2 domain specificity by controlling access to binding pockets. Kaneko T, Huang H, Zhao B, Li L, Liu H, Voss CK, Wu C, Schiller MR, Li SS. Sci Signal 3 ra34 (2010)
  4. Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates. Ng C, Jackson RA, Buschdorf JP, Sun Q, Guy GR, Sivaraman J. EMBO J. 27 804-816 (2008)
  5. Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation. Porter CJ, Matthews JM, Mackay JP, Pursglove SE, Schmidberger JW, Leedman PJ, Pero SC, Krag DN, Wilce MC, Wilce JA. BMC Struct. Biol. 7 58 (2007)
  6. Genome-wide prediction of SH2 domain targets using structural information and the FoldX algorithm. Sánchez IE, Beltrao P, Stricher F, Schymkowitz J, Ferkinghoff-Borg J, Rousseau F, Serrano L. PLoS Comput. Biol. 4 e1000052 (2008)
  7. LAT and NTAL mediate immunoglobulin E-induced sustained extracellular signal-regulated kinase activation critical for mast cell survival. Yamasaki S, Ishikawa E, Sakuma M, Kanagawa O, Cheng AM, Malissen B, Saito T. Mol. Cell. Biol. 27 4406-4415 (2007)
  8. SH2 domain containing leukocyte phosphoprotein of 76-kDa (SLP-76) feedback regulation of ZAP-70 microclustering. Liu H, Purbhoo MA, Davis DM, Rudd CE. Proc. Natl. Acad. Sci. U.S.A. 107 10166-10171 (2010)
  9. Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase Cgamma1. Deng L, Velikovsky CA, Swaminathan CP, Cho S, Mariuzza RA. J. Mol. Biol. 352 1-10 (2005)
  10. Modeling and simulation of aggregation of membrane protein LAT with molecular variability in the number of binding sites for cytosolic Grb2-SOS1-Grb2. Nag A, Monine M, Perelson AS, Goldstein B. PLoS ONE 7 e28758 (2012)
  11. Research Support, Non-U.S. Gov't LAT--an important raft-associated transmembrane adaptor protein. Delivered on 6 July 2009 at the 34th FEBS Congress in Prague, Czech Republic. Horejsí V, Otáhal P, Brdicka T. FEBS J. 277 4383-4397 (2010)
  12. T Cell Costimulation by CD6 Is Dependent on Bivalent Binding of a GADS/SLP-76 Complex. Breuning J, Brown MH. Mol. Cell. Biol. 37 (2017)
  13. Dimerization of the adaptor Gads facilitates antigen receptor signaling by promoting the cooperative binding of Gads to the adaptor LAT. Sukenik S, Frushicheva MP, Waknin-Lellouche C, Hallumi E, Ifrach T, Shalah R, Beach D, Avidan R, Oz I, Libman E, Aronheim A, Lewinson O, Yablonski D. Sci Signal 10 (2017)
  14. Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering. Moran O, Roessle MW, Mariuzza RA, Dimasi N. Biophys. J. 94 1766-1772 (2008)
  15. The development and application of a quantitative peptide microarray based approach to protein interaction domain specificity space. Engelmann BW, Kim Y, Wang M, Peters B, Rock RS, Nash PD. Mol. Cell Proteomics 13 3647-3662 (2014)
  16. Crystal Structures and Thermodynamic Analysis Reveal Distinct Mechanisms of CD28 Phosphopeptide Binding to the Src Homology 2 (SH2) Domains of Three Adaptor Proteins. Inaba S, Numoto N, Ogawa S, Morii H, Ikura T, Abe R, Ito N, Oda M. J. Biol. Chem. 292 1052-1060 (2017)
  17. Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction. Dimasi N. Int. J. Biochem. Cell Biol. 39 109-123 (2007)


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