The junctional adhesion molecule JAML is a costimulatory receptor for epithelial γδ T cell activation

Science

Volumn 329, Issue 5996, 2010, Pages 1205-1210

  Witherden, Deborah A ^a   Verdino, Petra ^a   Rieder, Stephanie E ^a,c   Garijo, Olivia ^a   Mills, Robyn E ^a,d   Teyton, Luc ^a   Fischer, Wolfgang H ^b   Wilson, Ian A ^a   Havran, Wendy L ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^c ABBOTT LABORATORIES   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

JUNCTIONAL ADHESION MOLECULE A; T LYMPHOCYTE RECEPTOR; T LYMPHOCYTE RECEPTOR DELTA CHAIN; VIRUS RECEPTOR; CELL ADHESION MOLECULE; CLMP PROTEIN, MOUSE; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR LIKE MEMBRANE PROTEIN; CYTOKINE; LIGAND; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BINDING; SIGNAL PEPTIDE;

ADHESION; BIOCHEMISTRY; CHEMICAL BINDING; CYTOLOGY; HOMEOSTASIS; LIGAND; PROTEIN;

ADENOVIRUS; ANIMAL CELL; ARTICLE; CELL PROLIFERATION; CELL STIMULATION; CONTROLLED STUDY; COXSACKIE VIRUS; CYTOKINE RELEASE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; T LYMPHOCYTE; T LYMPHOCYTE ACTIVATION; ANIMAL; C57BL MOUSE; CELL LINE; EPIDERMIS; EPITHELIUM; EPITHELIUM CELL; IMMUNOLOGY; KERATINOCYTE; LYMPHOCYTE ACTIVATION; METABOLISM; PROTEIN MOTIF; T LYMPHOCYTE SUBPOPULATION; WOUND HEALING;

AMINO ACID MOTIFS; ANIMALS; CELL ADHESION MOLECULES; CELL LINE; CELL PROLIFERATION; COXSACKIE AND ADENOVIRUS RECEPTOR-LIKE MEMBRANE PROTEIN; CYTOKINES; EPIDERMIS; EPITHELIAL CELLS; EPITHELIUM; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; KERATINOCYTES; LIGANDS; LYMPHOCYTE ACTIVATION; MICE; MICE, INBRED C57BL; PHOSPHATIDYLINOSITOL 3-KINASES; PROTEIN BINDING; RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA; RECEPTORS, VIRUS; T-LYMPHOCYTE SUBSETS; WOUND HEALING;

EID: 77956273963     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1192698     Document Type: Article

References (30)

1. W. L. Havran, Y. H. Chien, J. P. Allison, Science 252, 1430 (1991).
2. J. Jameson et al., Science 296, 747 (2002).
3. J. Strid, R. E. Tigelaar, A. C. Hayday, Semin. Immunol. 21, 110 (2009).
4. M. Girardi et al., Science 294, 605 (2001).
5. L. L. Sharp, J. M. Jameson, G. Cauvi, W. L. Havran, Nat. Immunol. 6, 73 (2005).
6. J. Jameson, W. L. Havran, Immunol. Rev. 215, 114 (2007).
7. A. C. Hayday, Annu. Rev. Immunol. 18, 975 (2000).
8. M. I. Whang, N. Guerra, D. H. Raulet, J. Immunol. 182, 4557 (2009).
9. Materials and methods are available as supporting material on Science Online.
10. C. Moog-Lutz et al., Blood 102, 3371 (2003).
11. A. C. Luissint, P. G. Lutz, D. A. Calderwood, P. O. Couraud, S. Bourdoulous, J. Cell Biol. 183, 1159 (2008).
12. G. Bazzoni, Curr. Opin. Cell Biol. 15, 525 (2003).
13. K. Ebnet, A. Suzuki, S. Ohno, D. Vestweber, J. Cell Sci. 117, 19 (2004).
14. A. J. Coyle et al., Immunity 13, 95 (2000).
15. M. Croft, C. Dubey, Crit. Rev. Immunol. 17, 89 (1997).
16. K. A. Frauwirth, C. B. Thompson, J. Clin. Invest. 109, 295 (2002).
17. K. Zen et al., Mol. Biol. Cell 16, 2694 (2005).
18. C. B. Coyne, J. M. Bergelson, Adv. Drug Deliv. Rev. 57, 869 (2005).
19. R. P. Tomko, R. Xu, L. Philipson, Proc. Natl. Acad. Sci. U.S.A. 94, 3352 (1997).
20. J. M. Bergelson et al., J. Virol. 72, 415 (1998).
21. J. Howitt, C. W. Anderson, P. Freimuth, Curr. Top. Microbiol. Immunol. 272, 331 (2003).
22. P. Verdino, D. A. Witherden, W. L. Havran, I. A. Wilson, Science 329, 1210 (2010).
23. I. Kirby et al., J. Virol. 75, 7210 (2001).
24. M. M. Davis et al., Annu. Rev. Biochem. 72, 717 (2003).
25. Single-letter abbreviations for the amino acid residues used in this report are as follows: Y, Tyr; M, Met; P, Pro; and X, any amino acid.
26. C. E. Rudd, H. Schneider, Nat. Rev. Immunol. 3, 544 (2003).
27. R. H. Schwartz, Science 248, 1349 (1990).
28. W. L. Havran, J. M. Jameson, J. Immunol. 184, 5423 (2010).
29. F5 and JAML recognize overlapping binding sites on CAR (22). As such, F5 is able to block the natural JAML-CAR interaction (Fig. 3, D and E).
30. We thank M. Park and W. Low for MS analysis; G. Nemerow for Fiber 5 and Fiber 11 reagents; J. Kaye for the DPK cell line; and M. Haynes, M. Svoboda, J. Barcas, K. Sendaydiego, D. Yeh, and B. Atteberry for technical assistance. J. Lewis provided advice on culture of short-term DETC lines. M. Kronenberg, R. Boismenu, J. Jameson, K. Mowen, T. Meehan, and K. Komori provided advice and critical reading of the manuscript. This work was supported by NIH grants to W.L.H. (AI52257, AI064811) and I.A.W. (AI42266, CA58896), as well as an Erwin- Schroedinger Fellowship of the Austrian Science Fund (P.V.) and the Leukemia and Lymphoma Society (S.E.R.). MS instrumentation was acquired with an NSF shared equipment grant. The MS Laboratory at the Salk Institute is supported by the Vincent J. Coates Foundation and NIH Blueprint NS057096. This is manuscript number 17711-IMM from The Scripps Research Institute.