Ca 2+ regulates T-cell receptor activation by modulating the charge property of lipids

Nature

Volumn 493, Issue 7430, 2013, Pages 111-115

  Shi, Xiaoshan ^a,b   Bi, Yunchen ^c   Yang, Wei ^a,b   Guo, Xingdong ^a,b   Jiang, Yan ^a,b   Wan, Chanjuan ^c   Li, Lunyi ^a,b   Bai, Yibing ^a,b   Guo, Jun ^a,b   Wang, Yujuan ^c   Chen, Xiangjun ^d   Wu, Bo ^c   Sun, Hongbin ^c   Liu, Wanli ^d   Wang, Junfeng ^c   Xu, Chenqi ^a,b  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

^c HEFEI INSTITUTES OF PHYSICAL SCIENCE   (China)

^d TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CD3 ANTIGEN; LIPID; STRONTIUM; T LYMPHOCYTE RECEPTOR; CALCIUM; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOLIPID; SOLVENT; TYROSINE;

ANTIGEN; CELL ORGANELLE; FLUORESCENCE SPECTROSCOPY; LIPID; MEMBRANE; NUCLEAR MAGNETIC RESONANCE; PHOSPHOLIPID; PROTEIN;

ANIMAL CELL; ARTICLE; CYTOPLASM; FLUORESCENCE RESONANCE ENERGY TRANSFER; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; T LYMPHOCYTE; ANIMAL; CELL MEMBRANE; CHEMISTRY; DRUG EFFECT; FEEDBACK SYSTEM; HUMAN; IMMUNOLOGY; LEUKEMIA CELL LINE; LIPID BILAYER; LYMPHOCYTE ACTIVATION; METABOLISM; PHOSPHORYLATION; SIGNAL TRANSDUCTION; STATIC ELECTRICITY;

ANIMALS; CALCIUM; CELL MEMBRANE; CYTOPLASM; FEEDBACK, PHYSIOLOGICAL; HUMANS; JURKAT CELLS; LIPID BILAYERS; LYMPHOCYTE ACTIVATION; MICE; PHOSPHOLIPIDS; PHOSPHORYLATION; RECEPTOR-CD3 COMPLEX, ANTIGEN, T-CELL; SIGNAL TRANSDUCTION; SOLVENTS; STATIC ELECTRICITY; T-LYMPHOCYTES; TYROSINE;

MLCS; MLOWN;

EID: 84871736291     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11699     Document Type: Article

References (31)

1. Xu, C. et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif. Cell 135, 702-713 (2008).
2. Paddock, C. et al. Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation. Blood 117, 6012-6023 (2011).
3. Hansen, S. B., Tao, X. & MacKinnon, R. Structural basis of PIP2 activation of the classical inward rectifier K1 channel Kir2.2. Nature 477, 495-498 (2011).
4. Whorton, M. R. & MacKinnon, R. Crystal structure of the mammalian GIRK2 K1 channel and gating regulation byGproteins, PIP2,andsodium. Cell147, 199-208 (2011).
5. Kim, C. et al. Basic amino-acid side chains regulate transmembrane integrin signalling. Nature 481, 209-213 (2012).
6. van den Bogaart, G. et al. Membrane protein sequestering by ionic protein-lipid interactions. Nature 479, 552-555 (2011).
7. Heo, W. D. et al. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314, 1458-1461 (2006).
8. Kuhns, M. S. & Davis, M. M. The safety on the TCR trigger. Cell 135, 594-596 (2008).
9. DeFord-Watts, L. M. et al. The CD3f subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse. J. Immunol. 186, 6839-6847 (2011).
10. Aivazian, D. & Stern, L. J. Phosphorylation of T cell receptor f is regulated by a lipid dependent folding transition. Nature Struct. Biol. 7, 1023-1026 (2000).
11. Irvine, D. J., Purbhoo, M. A., Krogsgaard, M. & Davis, M. M. Direct observation of ligand recognition by T cells. Nature 419, 845-849 (2002). (Pubitemid 35238571)
12. Lioudyno, M. I. et al. Orai1 and STIM1 move to the immunological synapse and are up-regulated during T cell activation. Proc. Natl Acad. Sci. USA 105, 2011-2016 (2008). (Pubitemid 351439456)
13. Smith-Garvin, J. E., Koretzky, G. A. & Jordan, M. S. T cell activation. Annu. Rev. Immunol. 27, 591-619 (2009).
14. Palacios, E. H. & Weiss, A. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 23, 7990-8000 (2004). (Pubitemid 39468856)
15. Hogan, P. G., Lewis, R. S. & Rao, A. Molecular basis of calcium signaling in lymphocytes: STIM and ORAI. Annu. Rev. Immunol. 28, 491-533 (2010).
16. Weiss, A. & Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274 (1994). (Pubitemid 24046689)
17. van derMerwe, P. A.&Dushek, O.Mechanismsfor T cell receptor triggering. Nature Rev. Immunol. 11, 47-55 (2011).
18. Purbhoo, M. A., Irvine, D. J., Huppa, J. B.& Davis, M. M. T cell killing does not require the formation of a stable mature immunological synapse. Nature Immunol. 5, 524-530 (2004). (Pubitemid 38660465)
19. Sigalov, A. B., Aivazian, D. A., Uversky, V. N. & Stern, L. J. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry 45, 15731-15739 (2006). (Pubitemid 46032493)
20. Leventis, P.A.&Grinstein, S. The distribution andfunction ofphosphatidylserine in cellular membranes. Annu. Rev. Biophys. 39, 407-427 (2010).
21. Nika, K. et al. Constitutively active Lck kinase in T cells drives antigen receptor signal transduction. Immunity 32, 766-777 (2010).
22. Huse, M. et al. Spatial and temporal dynamics of T cell receptor signaling with a photoactivatable agonist. Immunity 27, 76-88 (2007). (Pubitemid 47089024)
23. Fanger, C. M., Hoth, M., Crabtree, G. R. & Lewis, R. S. Characterization of T cell mutants with defects in capacitative calcium entry: genetic evidence for the physiological roles of CRAC channels. J. Cell Biol. 131, 655-667 (1995).
24. Park, C. Y., Shcheglovitov, A. & Dolmetsch, R. The CRAC channel activator STIM1 binds and inhibits L-type voltage-gated calcium channels. Science 330, 101-105 (2010).
25. Yeromin, A. V. et al. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 443, 226-229 (2006). (Pubitemid 44387612)
26. Denisov, I. G., Grinkova, Y. V., Lazarides, A. A.&Sligar, S. G. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126, 3477-3487 (2004). (Pubitemid 38366738)
27. Quintana, A. et al. Calcium microdomains at the immunological synapse: how ORAI channels, mitochondria and calcium pumps generate local calcium signals for efficient T-cell activation. EMBO J. 30, 3895-3912 (2011).
28. Varma, R., Campi, G., Yokosuka, T., Saito, T. & Dustin, M. L. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 25, 117-127 (2006). (Pubitemid 44066825)
29. Huppa, J. B., Gleimer, M., Sumen, C. & Davis, M. M. Continuous T cell receptor signaling required for synapse maintenance and full effector potential. Nature Immunol. 4, 749-755 (2003). (Pubitemid 36986758)
30. Zilly, F. E. et al. Ca21 induces clustering of membrane proteins in the plasma membrane via electrostatic interactions. EMBO J. 30, 1209-1220 (2011).
31. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).