메뉴 건너뛰기




Volumn 116, Issue 2, 2008, Pages 117-125

A biophysical approach to IL-2 and IL-15 receptor function: Localization, conformation and interactions

Author keywords

Confocal microscopy; Fluorescence correlation spectroscopy; FRET; IL 2 and IL 15 receptors; Near field scanning optical microscopy; Protein protein interactions; Receptor patterns; Structure determination; X ray crystallography

Indexed keywords

INTERLEUKIN 15 RECEPTOR; INTERLEUKIN 2 RECEPTOR;

EID: 40349103692     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2007.12.014     Document Type: Review
Times cited : (36)

References (109)
  • 1
    • 0025102756 scopus 로고
    • Haemopoietic receptors and helical cytokines
    • Bazan J.F. Haemopoietic receptors and helical cytokines. Immunol Today 11 (1990) 350-354
    • (1990) Immunol Today , vol.11 , pp. 350-354
    • Bazan, J.F.1
  • 2
    • 0033491981 scopus 로고    scopus 로고
    • Biology of the interleukin-2 receptor
    • Nelson B.H., and Willerford D.M. Biology of the interleukin-2 receptor. Adv Immunol 70 (1998) 1-81
    • (1998) Adv Immunol , vol.70 , pp. 1-81
    • Nelson, B.H.1    Willerford, D.M.2
  • 3
    • 0035169507 scopus 로고    scopus 로고
    • Interleukin 15: biology and relevance to human disease
    • Fehniger T.A., and Caligiuri M.A. Interleukin 15: biology and relevance to human disease. Blood 97 (2001) 14-32
    • (2001) Blood , vol.97 , pp. 14-32
    • Fehniger, T.A.1    Caligiuri, M.A.2
  • 4
    • 0027731604 scopus 로고
    • Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4
    • Kondo M., Takeshita T., Ishii N., Nakamura M., Watanabe S., Arai K., et al. Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4. Science 262 (1993) 1874-1877
    • (1993) Science , vol.262 , pp. 1874-1877
    • Kondo, M.1    Takeshita, T.2    Ishii, N.3    Nakamura, M.4    Watanabe, S.5    Arai, K.6
  • 5
    • 0028327550 scopus 로고
    • Functional participation of the IL-2 receptor gamma chain in IL-7 receptor complexes
    • Kondo M., Takeshita T., Higuchi M., Nakamura M., Sudo T., Nishikawa S., et al. Functional participation of the IL-2 receptor gamma chain in IL-7 receptor complexes. Science 263 (1994) 1453-1454
    • (1994) Science , vol.263 , pp. 1453-1454
    • Kondo, M.1    Takeshita, T.2    Higuchi, M.3    Nakamura, M.4    Sudo, T.5    Nishikawa, S.6
  • 7
    • 0028814556 scopus 로고
    • Sharing of the IL-2 receptor gamma chain with the functional IL-9 receptor complex
    • Kimura Y., Takeshita T., Kondo M., Ishii N., Nakamura M., Van S.J., et al. Sharing of the IL-2 receptor gamma chain with the functional IL-9 receptor complex. Int Immunol 7 (1995) 115-120
    • (1995) Int Immunol , vol.7 , pp. 115-120
    • Kimura, Y.1    Takeshita, T.2    Kondo, M.3    Ishii, N.4    Nakamura, M.5    Van, S.J.6
  • 8
    • 0035814926 scopus 로고    scopus 로고
    • Cytokines: IL-21 joins the gamma(c)-dependent network?
    • Vosshenrich C.A., and Di Santo J.P. Cytokines: IL-21 joins the gamma(c)-dependent network?. Curr Biol 11 (2001) R175-R177
    • (2001) Curr Biol , vol.11
    • Vosshenrich, C.A.1    Di Santo, J.P.2
  • 9
    • 0031194890 scopus 로고    scopus 로고
    • Cytokines: shared receptors, distinct functions
    • DiSanto J.P. Cytokines: shared receptors, distinct functions. Curr Biol 7 (1997) R424-R426
    • (1997) Curr Biol , vol.7
    • DiSanto, J.P.1
  • 10
    • 0028363377 scopus 로고
    • The interleukin (IL) 2 receptor beta chain is shared by IL-2 and a cytokine, provisionally designated IL-T, that stimulates T-cell proliferation and the induction of lymphokine-activated killer cells
    • Bamford R.N., Grant A.J., Burton J.D., Peters C., Kurys G., Goldman C.K., et al. The interleukin (IL) 2 receptor beta chain is shared by IL-2 and a cytokine, provisionally designated IL-T, that stimulates T-cell proliferation and the induction of lymphokine-activated killer cells. Proc Natl Acad Sci USA 91 (1994) 4940-4944
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4940-4944
    • Bamford, R.N.1    Grant, A.J.2    Burton, J.D.3    Peters, C.4    Kurys, G.5    Goldman, C.K.6
  • 11
    • 0028221433 scopus 로고
    • Utilization of the beta and gamma chains of the IL-2 receptor by the novel cytokine IL-15
    • Giri J.G., Ahdieh M., Eisenman J., Shanebeck K., Grabstein K., Kumaki S., et al. Utilization of the beta and gamma chains of the IL-2 receptor by the novel cytokine IL-15. EMBO J 13 (1994) 2822-2830
    • (1994) EMBO J , vol.13 , pp. 2822-2830
    • Giri, J.G.1    Ahdieh, M.2    Eisenman, J.3    Shanebeck, K.4    Grabstein, K.5    Kumaki, S.6
  • 12
    • 0028179054 scopus 로고
    • Cloning of a T cell growth factor that interacts with the beta chain of the interleukin-2 receptor
    • Grabstein K.H., Eisenman J., Shanebeck K., Rauch C., Srinivasan S., Fung V., et al. Cloning of a T cell growth factor that interacts with the beta chain of the interleukin-2 receptor. Science 264 (1994) 965-968
    • (1994) Science , vol.264 , pp. 965-968
    • Grabstein, K.H.1    Eisenman, J.2    Shanebeck, K.3    Rauch, C.4    Srinivasan, S.5    Fung, V.6
  • 13
    • 0025778240 scopus 로고
    • The interleukin-2 receptor
    • Waldmann T.A. The interleukin-2 receptor. J Biol Chem 266 (1991) 2681-2684
    • (1991) J Biol Chem , vol.266 , pp. 2681-2684
    • Waldmann, T.A.1
  • 15
    • 0029099146 scopus 로고
    • Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor
    • Giri J.G., Kumaki S., Ahdieh M., Friend D.J., Loomis A., Shanebeck K., et al. Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. EMBO J 14 (1995) 3654-3663
    • (1995) EMBO J , vol.14 , pp. 3654-3663
    • Giri, J.G.1    Kumaki, S.2    Ahdieh, M.3    Friend, D.J.4    Loomis, A.5    Shanebeck, K.6
  • 16
    • 13344278015 scopus 로고
    • Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes
    • Anderson D.M., Kumaki S., Ahdieh M., Bertles J., Tometsko M., Loomis A., et al. Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes. J Biol Chem 270 (1995) 29862-29869
    • (1995) J Biol Chem , vol.270 , pp. 29862-29869
    • Anderson, D.M.1    Kumaki, S.2    Ahdieh, M.3    Bertles, J.4    Tometsko, M.5    Loomis, A.6
  • 17
    • 0028286627 scopus 로고
    • Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling
    • Nakamura Y., Russell S.M., Mess S.A., Friedmann M., Erdos M., Francois C., et al. Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling. Nature 369 (1994) 330-333
    • (1994) Nature , vol.369 , pp. 330-333
    • Nakamura, Y.1    Russell, S.M.2    Mess, S.A.3    Friedmann, M.4    Erdos, M.5    Francois, C.6
  • 18
    • 0029115522 scopus 로고
    • Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15
    • Johnston J.A., Bacon C.M., Finbloom D.S., Rees R.C., Kaplan D., Shibuya K., et al. Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15. Proc Natl Acad Sci USA 92 (1995) 8705-8709
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8705-8709
    • Johnston, J.A.1    Bacon, C.M.2    Finbloom, D.S.3    Rees, R.C.4    Kaplan, D.5    Shibuya, K.6
  • 19
    • 0028962572 scopus 로고
    • The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15
    • Lin J.X., Migone T.S., Tsang M., Friedmann M., Weatherbee J.A., Zhou L., et al. The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15. Immunity 2 (1995) 331-339
    • (1995) Immunity , vol.2 , pp. 331-339
    • Lin, J.X.1    Migone, T.S.2    Tsang, M.3    Friedmann, M.4    Weatherbee, J.A.5    Zhou, L.6
  • 20
    • 0029054455 scopus 로고
    • Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation
    • Miyazaki T., Liu Z.J., Kawahara A., Minami Y., Yamada K., Tsujimoto Y., et al. Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. Cell 81 (1995) 223-231
    • (1995) Cell , vol.81 , pp. 223-231
    • Miyazaki, T.1    Liu, Z.J.2    Kawahara, A.3    Minami, Y.4    Yamada, K.5    Tsujimoto, Y.6
  • 21
    • 0032876816 scopus 로고    scopus 로고
    • Death deflected: IL-15 inhibits TNF-alpha-mediated apoptosis in fibroblasts by TRAF2 recruitment to the IL-15Ralpha chain
    • Bulfone-PauS S., Bulanova E., Pohl T., Budagian V., Durkop H., and Ruckert R. Death deflected: IL-15 inhibits TNF-alpha-mediated apoptosis in fibroblasts by TRAF2 recruitment to the IL-15Ralpha chain. FASEB J 13 (1999) 1575-1585
    • (1999) FASEB J , vol.13 , pp. 1575-1585
    • Bulfone-PauS, S.1    Bulanova, E.2    Pohl, T.3    Budagian, V.4    Durkop, H.5    Ruckert, R.6
  • 22
    • 0035576258 scopus 로고    scopus 로고
    • The IL-15R alpha chain signals through association with Syk in human B cells
    • Bulanova E., Budagian V., Pohl T., Krause H., Durkop H., Paus R., et al. The IL-15R alpha chain signals through association with Syk in human B cells. J Immunol 167 (2001) 6292-6302
    • (2001) J Immunol , vol.167 , pp. 6292-6302
    • Bulanova, E.1    Budagian, V.2    Pohl, T.3    Krause, H.4    Durkop, H.5    Paus, R.6
  • 23
    • 0030969845 scopus 로고    scopus 로고
    • Interleukin-15 signals T84 colonic epithelial cells in the absence of the interleukin-2 receptor beta-chain
    • Stevens A.C., Matthews J., Andres P., Baffis V., Zheng X.X., Chae D.W., et al. Interleukin-15 signals T84 colonic epithelial cells in the absence of the interleukin-2 receptor beta-chain. Am J Physiol 272 (1997) G1201-G1208
    • (1997) Am J Physiol , vol.272
    • Stevens, A.C.1    Matthews, J.2    Andres, P.3    Baffis, V.4    Zheng, X.X.5    Chae, D.W.6
  • 25
    • 0036826914 scopus 로고    scopus 로고
    • IL-15Ralpha recycles and presents IL-15 in trans to neighboring cells
    • Dubois S., Mariner J., Waldmann T.A., and Tagaya Y. IL-15Ralpha recycles and presents IL-15 in trans to neighboring cells. Immunity 17 (2002) 537-547
    • (2002) Immunity , vol.17 , pp. 537-547
    • Dubois, S.1    Mariner, J.2    Waldmann, T.A.3    Tagaya, Y.4
  • 26
    • 19344368323 scopus 로고    scopus 로고
    • The roles of interleukin-15 receptor alpha: trans-presentation, receptor component, or both?
    • Schluns K.S., Stoklasek T., and Lefrancois L. The roles of interleukin-15 receptor alpha: trans-presentation, receptor component, or both?. Int J Biochem Cell Biol 37 (2005) 1567-1571
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1567-1571
    • Schluns, K.S.1    Stoklasek, T.2    Lefrancois, L.3
  • 27
    • 0035102242 scopus 로고    scopus 로고
    • Contrasting roles of IL-2 and IL-15 in the life and death of lymphocytes: implications for immunotherapy
    • Waldmann T.A., Dubois S., and Tagaya Y. Contrasting roles of IL-2 and IL-15 in the life and death of lymphocytes: implications for immunotherapy. Immunity 14 (2001) 105-110
    • (2001) Immunity , vol.14 , pp. 105-110
    • Waldmann, T.A.1    Dubois, S.2    Tagaya, Y.3
  • 28
    • 0033046593 scopus 로고    scopus 로고
    • The multifaceted regulation of interleukin-15 expression and the role of this cytokine in NK cell differentiation and host response to intracellular pathogens
    • Waldmann T.A., and Tagaya Y. The multifaceted regulation of interleukin-15 expression and the role of this cytokine in NK cell differentiation and host response to intracellular pathogens. Annu Rev Immunol 17 (1999) 19-49
    • (1999) Annu Rev Immunol , vol.17 , pp. 19-49
    • Waldmann, T.A.1    Tagaya, Y.2
  • 29
    • 0001585396 scopus 로고    scopus 로고
    • Control of homeostasis of CD8+ memory T cells by opposing cytokines
    • Ku C.C., Murakami M., Sakamoto A., Kappler J., and Marrack P. Control of homeostasis of CD8+ memory T cells by opposing cytokines. Science 288 (2000) 675-678
    • (2000) Science , vol.288 , pp. 675-678
    • Ku, C.C.1    Murakami, M.2    Sakamoto, A.3    Kappler, J.4    Marrack, P.5
  • 31
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions
    • Berggard T., Linse S., and James P. Methods for the detection and analysis of protein-protein interactions. Proteomics 7 (2007) 2833-2842
    • (2007) Proteomics , vol.7 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 32
    • 0032190410 scopus 로고    scopus 로고
    • Supramolecular receptor structures in the plasma membrane of lymphocytes revealed by flow cytometric energy transfer, scanning force- and transmission electron-microscopic analyses
    • Damjanovich S., Matkó J., Mátyus L., Szabo Jr. G., Szöllo{combining double acute accent}si J., Pieri J.C., et al. Supramolecular receptor structures in the plasma membrane of lymphocytes revealed by flow cytometric energy transfer, scanning force- and transmission electron-microscopic analyses. Cytometry 33 (1998) 225-233
    • (1998) Cytometry , vol.33 , pp. 225-233
    • Damjanovich, S.1    Matkó, J.2    Mátyus, L.3    Szabo Jr., G.4    Szöllosi, J.5    Pieri, J.C.6
  • 34
    • 40349088256 scopus 로고    scopus 로고
    • Non-random patterns of membrane proteins and their roles in transmembrane signaling
    • Damjanovich S. (Ed), Springer-Verlag, Berlin, Heidelberg
    • Bodnár A., Vámosi G., Toth K., Jenei A., Mátyus L., and Damjanovich S. Non-random patterns of membrane proteins and their roles in transmembrane signaling. In: Damjanovich S. (Ed). Biophysical aspects of transmembrane signaling (2005), Springer-Verlag, Berlin, Heidelberg 71-95
    • (2005) Biophysical aspects of transmembrane signaling , pp. 71-95
    • Bodnár, A.1    Vámosi, G.2    Toth, K.3    Jenei, A.4    Mátyus, L.5    Damjanovich, S.6
  • 35
    • 40349112381 scopus 로고    scopus 로고
    • Role of lipid microdomains in the formation of supramolecular protein complexes and transmembrane signaling
    • Fielding C.J. (Ed), Wiley-VCH Verlag, Weinheim
    • Vámosi G., Bodnár A., Vereb G., Szöllo{combining double acute accent}si J., and Damjanovich S. Role of lipid microdomains in the formation of supramolecular protein complexes and transmembrane signaling. In: Fielding C.J. (Ed). Lipid rafts and caveolae (2006), Wiley-VCH Verlag, Weinheim 141-174
    • (2006) Lipid rafts and caveolae , pp. 141-174
    • Vámosi, G.1    Bodnár, A.2    Vereb, G.3    Szöllosi, J.4    Damjanovich, S.5
  • 36
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster T. Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann Phys 2 (1948) 55-75
    • (1948) Ann Phys , vol.2 , pp. 55-75
    • Förster, T.1
  • 37
    • 0000287353 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET)
    • Wang X.F., and Herman B. (Eds), Wiley, John & Sons, Inc., New York
    • Clegg R.M. Fluorescence resonance energy transfer (FRET). In: Wang X.F., and Herman B. (Eds). Fluorescence Imaging Spectroscopy and Microscopy. (1996), Wiley, John & Sons, Inc., New York
    • (1996) Fluorescence Imaging Spectroscopy and Microscopy.
    • Clegg, R.M.1
  • 38
    • 0021273333 scopus 로고
    • Flow cytometric measurements of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell by cell basis
    • Tron L., Szöllösi J., Damjanovich S., Helliwell S.H., Arndt-Jovin D.J., and Jovin T.M. Flow cytometric measurements of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell by cell basis. Biophys J 45 (1984) 939-946
    • (1984) Biophys J , vol.45 , pp. 939-946
    • Tron, L.1    Szöllösi, J.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.J.5    Jovin, T.M.6
  • 39
    • 0036628631 scopus 로고    scopus 로고
    • Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer
    • Sebestyén Z., Nagy P., Horváth G., Vámosi G., Debets R., Gratama J.W., et al. Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer. Cytometry 48 (2002) 124-135
    • (2002) Cytometry , vol.48 , pp. 124-135
    • Sebestyén, Z.1    Nagy, P.2    Horváth, G.3    Vámosi, G.4    Debets, R.5    Gratama, J.W.6
  • 40
    • 3242784810 scopus 로고    scopus 로고
    • Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis
    • Szentesi G., Horvath G., Bori I., Vámosi G., Szöllo{combining double acute accent}si J., Gáspár R., et al. Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis. Comput Methods Programs Biomed 75 (2004) 201-211
    • (2004) Comput Methods Programs Biomed , vol.75 , pp. 201-211
    • Szentesi, G.1    Horvath, G.2    Bori, I.3    Vámosi, G.4    Szöllosi, J.5    Gáspár, R.6
  • 41
    • 0344447088 scopus 로고    scopus 로고
    • Intensity-based energy transfer measurements in digital imaging microscopy
    • Nagy P., Vámosi G., Bodnár A., Lockett S.J., and Szöllo{combining double acute accent}si J. Intensity-based energy transfer measurements in digital imaging microscopy. Eur Biophys J 27 (1998) 377-389
    • (1998) Eur Biophys J , vol.27 , pp. 377-389
    • Nagy, P.1    Vámosi, G.2    Bodnár, A.3    Lockett, S.J.4    Szöllosi, J.5
  • 42
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella Jr. T.W., and Jovin T.M. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J Cell Biol 129 (1995) 1543-1558
    • (1995) J Cell Biol , vol.129 , pp. 1543-1558
    • Gadella Jr., T.W.1    Jovin, T.M.2
  • 43
    • 0028023293 scopus 로고
    • Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics
    • Young R.M., Arnette J.K., Roess D.A., and Barisas B.G. Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics. Biophys J 67 (1994) 881-888
    • (1994) Biophys J , vol.67 , pp. 881-888
    • Young, R.M.1    Arnette, J.K.2    Roess, D.A.3    Barisas, B.G.4
  • 44
    • 3342924000 scopus 로고    scopus 로고
    • IL-2 and IL-15 receptor alpha-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells
    • Vámosi G., Bodnár A., Vereb G., Jenei A., Goldman C.K., Langowski J., et al. IL-2 and IL-15 receptor alpha-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells. Proc Natl Acad Sci USA 101 (2004) 11082-11087
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11082-11087
    • Vámosi, G.1    Bodnár, A.2    Vereb, G.3    Jenei, A.4    Goldman, C.K.5    Langowski, J.6
  • 45
    • 41649101278 scopus 로고    scopus 로고
    • Conformation of the c-Fos/c-Jun complex in vivo: a combined FRET, FCCS and MD-modeling study
    • (PMID: 18065450)
    • Vámosi G., Baudendistel N., von der Lieth C.W., Szaloki N., Mocsar G., Muller G., et al. Conformation of the c-Fos/c-Jun complex in vivo: a combined FRET, FCCS and MD-modeling study. Biophys J (2007) (PMID: 18065450)
    • (2007) Biophys J
    • Vámosi, G.1    Baudendistel, N.2    von der Lieth, C.W.3    Szaloki, N.4    Mocsar, G.5    Muller, G.6
  • 46
    • 0033014064 scopus 로고    scopus 로고
    • Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy
    • Nagy P., Jenei A., Kirsch A.K., Szöllo{combining double acute accent}si J., Damjanovich S., and Jovin T.M. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J Cell Sci 112 Pt 11 (1999) 1733-1741
    • (1999) J Cell Sci , vol.112 , Issue.PART 11 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Szöllosi, J.4    Damjanovich, S.5    Jovin, T.M.6
  • 47
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • Bacia K., Kim S.A., and Schwille P. Fluorescence cross-correlation spectroscopy in living cells. Nat Methods 3 (2006) 83-89
    • (2006) Nat Methods , vol.3 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 48
    • 0036793231 scopus 로고    scopus 로고
    • Crystal structures of alpha-helical cytokine-receptor complexes: we've only scratched the surface
    • Walter M.R. Crystal structures of alpha-helical cytokine-receptor complexes: we've only scratched the surface. Biotechniques Suppl. (2002) 46-47
    • (2002) Biotechniques , Issue.SUPPL , pp. 46-47
    • Walter, M.R.1
  • 49
    • 0028674451 scopus 로고
    • Multidimensional heteronuclear nuclear magnetic resonance of proteins
    • Clore G.M., and Gronenborn A.M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol 239 (1994) 349-363
    • (1994) Methods Enzymol , vol.239 , pp. 349-363
    • Clore, G.M.1    Gronenborn, A.M.2
  • 50
    • 0032720858 scopus 로고    scopus 로고
    • Biosensor analysis of the interleukin-2 receptor complex
    • Liparoto S.F., and Ciardelli T.L. Biosensor analysis of the interleukin-2 receptor complex. J Mol Recognit 12 (1999) 316-321
    • (1999) J Mol Recognit , vol.12 , pp. 316-321
    • Liparoto, S.F.1    Ciardelli, T.L.2
  • 51
    • 33847770317 scopus 로고    scopus 로고
    • SPR microscopy and its applications to high-throughput analyses of biomolecular binding events and their kinetics
    • Campbell C.T., and Kim G. SPR microscopy and its applications to high-throughput analyses of biomolecular binding events and their kinetics. Biomaterials 28 (2007) 2380-2392
    • (2007) Biomaterials , vol.28 , pp. 2380-2392
    • Campbell, C.T.1    Kim, G.2
  • 52
    • 33746547247 scopus 로고    scopus 로고
    • The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design
    • Waldmann T.A. The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design. Nat Rev Immunol 6 (2006) 595-601
    • (2006) Nat Rev Immunol , vol.6 , pp. 595-601
    • Waldmann, T.A.1
  • 53
    • 0033578642 scopus 로고    scopus 로고
    • Natural splicing of exon 2 of human interleukin-15 receptor alpha-chain mRNA results in a shortened form with a distinct pattern of expression
    • Dubois S., Magrangeas F., Lehours P., Raher S., Bernard J., Boisteau O., et al. Natural splicing of exon 2 of human interleukin-15 receptor alpha-chain mRNA results in a shortened form with a distinct pattern of expression. J Biol Chem 274 (1999) 26978-26984
    • (1999) J Biol Chem , vol.274 , pp. 26978-26984
    • Dubois, S.1    Magrangeas, F.2    Lehours, P.3    Raher, S.4    Bernard, J.5    Boisteau, O.6
  • 54
    • 0025894780 scopus 로고
    • Three-dimensional structure of a complement control protein module in solution
    • Norman D.G., Barlow P.N., Baron M., Day A.J., Sim R.B., and Campbell I.D. Three-dimensional structure of a complement control protein module in solution. J Mol Biol 219 (1991) 717-725
    • (1991) J Mol Biol , vol.219 , pp. 717-725
    • Norman, D.G.1    Barlow, P.N.2    Baron, M.3    Day, A.J.4    Sim, R.B.5    Campbell, I.D.6
  • 55
    • 0035399559 scopus 로고    scopus 로고
    • The Sushi domain of soluble IL-15 receptor alpha is essential for binding IL-15 and inhibiting inflammatory and allogenic responses in vitro and in vivo
    • Wei X., Orchardson M., Gracie J.A., Leung B.P., Gao B., Guan H., et al. The Sushi domain of soluble IL-15 receptor alpha is essential for binding IL-15 and inhibiting inflammatory and allogenic responses in vitro and in vivo. J Immunol 167 (2001) 277-282
    • (2001) J Immunol , vol.167 , pp. 277-282
    • Wei, X.1    Orchardson, M.2    Gracie, J.A.3    Leung, B.P.4    Gao, B.5    Guan, H.6
  • 56
    • 33644975335 scopus 로고    scopus 로고
    • Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 × IL-15R alpha fusion proteins
    • Mortier E., Quemener A., Vusio P., Lorenzen I., Boublik Y., Grotzinger J., et al. Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 × IL-15R alpha fusion proteins. J Biol Chem 281 (2006) 1612-1619
    • (2006) J Biol Chem , vol.281 , pp. 1612-1619
    • Mortier, E.1    Quemener, A.2    Vusio, P.3    Lorenzen, I.4    Boublik, Y.5    Grotzinger, J.6
  • 57
    • 20344387872 scopus 로고    scopus 로고
    • The structure of interleukin-2 complexed with its alpha receptor
    • Rickert M., Wang X., Boulanger M.J., Goriatcheva N., and Garcia K.C. The structure of interleukin-2 complexed with its alpha receptor. Science 308 (2005) 1477-1480
    • (2005) Science , vol.308 , pp. 1477-1480
    • Rickert, M.1    Wang, X.2    Boulanger, M.J.3    Goriatcheva, N.4    Garcia, K.C.5
  • 58
    • 33644540157 scopus 로고    scopus 로고
    • Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor
    • Stauber D.J., Debler E.W., Horton P.A., Smith K.A., and Wilson I.A. Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor. Proc Natl Acad Sci USA 103 (2006) 2788-2793
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2788-2793
    • Stauber, D.J.1    Debler, E.W.2    Horton, P.A.3    Smith, K.A.4    Wilson, I.A.5
  • 59
    • 27944505913 scopus 로고    scopus 로고
    • Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors
    • Wang X., Rickert M., and Garcia K.C. Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors. Science 310 (2005) 1159-1163
    • (2005) Science , vol.310 , pp. 1159-1163
    • Wang, X.1    Rickert, M.2    Garcia, K.C.3
  • 60
    • 33646580769 scopus 로고    scopus 로고
    • The structure of the interleukin-15 alpha receptor and its implications for ligand binding
    • Lorenzen I., Dingley A.J., Jacques Y., and Grotzinger J. The structure of the interleukin-15 alpha receptor and its implications for ligand binding. J Biol Chem 281 (2006) 6642-6647
    • (2006) J Biol Chem , vol.281 , pp. 6642-6647
    • Lorenzen, I.1    Dingley, A.J.2    Jacques, Y.3    Grotzinger, J.4
  • 61
    • 2642522073 scopus 로고    scopus 로고
    • Identification of an interleukin-15alpha receptor-binding site on human interleukin-15
    • Bernard J., Harb C., Mortier E., Quemener A., Meloen R.H., Vermot-Desroches C., et al. Identification of an interleukin-15alpha receptor-binding site on human interleukin-15. J Biol Chem 279 (2004) 24313-24322
    • (2004) J Biol Chem , vol.279 , pp. 24313-24322
    • Bernard, J.1    Harb, C.2    Mortier, E.3    Quemener, A.4    Meloen, R.H.5    Vermot-Desroches, C.6
  • 62
    • 34548125264 scopus 로고    scopus 로고
    • Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in trans
    • Chirifu M., Hayashi C., Nakamura T., Toma S., Shuto T., Kai H., et al. Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in trans. Nat Immunol 8 (2007) 1001-1007
    • (2007) Nat Immunol , vol.8 , pp. 1001-1007
    • Chirifu, M.1    Hayashi, C.2    Nakamura, T.3    Toma, S.4    Shuto, T.5    Kai, H.6
  • 63
    • 3042538263 scopus 로고    scopus 로고
    • Compensatory energetic mechanisms mediating the assembly of signaling complexes between interleukin-2 and its alpha, beta, and gamma(c) receptors
    • Rickert M., Boulanger M.J., Goriatcheva N., and Garcia K.C. Compensatory energetic mechanisms mediating the assembly of signaling complexes between interleukin-2 and its alpha, beta, and gamma(c) receptors. J Mol Biol 339 (2004) 1115-1128
    • (2004) J Mol Biol , vol.339 , pp. 1115-1128
    • Rickert, M.1    Boulanger, M.J.2    Goriatcheva, N.3    Garcia, K.C.4
  • 64
    • 37549007225 scopus 로고    scopus 로고
    • Crystal structure of the interleukin-15 interleukin-15 receptor alpha complex: insights into trans and cis presentation
    • Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K., Uchiyama H., et al. Crystal structure of the interleukin-15 interleukin-15 receptor alpha complex: insights into trans and cis presentation. J Biol Chem (2007)
    • (2007) J Biol Chem
    • Olsen, S.K.1    Ota, N.2    Kishishita, S.3    Kukimoto-Niino, M.4    Murayama, K.5    Uchiyama, H.6
  • 65
    • 0026021208 scopus 로고
    • Synergistic action of monoclonal antibodies directed at p55 and p75 chains of the human IL-2-receptor
    • Audrain M., Boeffard F., Soulillou J.P., and Jacques Y. Synergistic action of monoclonal antibodies directed at p55 and p75 chains of the human IL-2-receptor. J Immunol 146 (1991) 884-892
    • (1991) J Immunol , vol.146 , pp. 884-892
    • Audrain, M.1    Boeffard, F.2    Soulillou, J.P.3    Jacques, Y.4
  • 66
    • 0025339533 scopus 로고
    • Role of alpha chain-IL-2 complex in the formation of the ternary complex of IL-2 and high-affinity IL-2 receptor
    • Kamio M., Uchiyama T., Arima N., Itoh K., Ishikawa T., Hori T., et al. Role of alpha chain-IL-2 complex in the formation of the ternary complex of IL-2 and high-affinity IL-2 receptor. Int Immunol 2 (1990) 521-530
    • (1990) Int Immunol , vol.2 , pp. 521-530
    • Kamio, M.1    Uchiyama, T.2    Arima, N.3    Itoh, K.4    Ishikawa, T.5    Hori, T.6
  • 67
    • 0025609656 scopus 로고
    • Stepwise formation of the high-affinity complex of the interleukin 2 receptor
    • Saito Y., Ogura T., Kamio M., Sabe H., Uchiyama T., and Honjo T. Stepwise formation of the high-affinity complex of the interleukin 2 receptor. Int Immunol 2 (1990) 1167-1177
    • (1990) Int Immunol , vol.2 , pp. 1167-1177
    • Saito, Y.1    Ogura, T.2    Kamio, M.3    Sabe, H.4    Uchiyama, T.5    Honjo, T.6
  • 68
    • 0023681759 scopus 로고
    • Direct identification of the murine IL-2 receptor p55-p75 heterodimer in the absence of IL-2
    • Saragovi H., and Malek T.R. Direct identification of the murine IL-2 receptor p55-p75 heterodimer in the absence of IL-2. J Immunol 141 (1988) 476-482
    • (1988) J Immunol , vol.141 , pp. 476-482
    • Saragovi, H.1    Malek, T.R.2
  • 69
    • 0024448768 scopus 로고
    • Structure of the functional interleukin-2 receptor. Evidence for the association of human p55 and murine p75 molecules in a mouse T cell line
    • Yamaguchi A., Ide T., Hatakeyama M., Doi T., Kono T., Uchiyama T., et al. Structure of the functional interleukin-2 receptor. Evidence for the association of human p55 and murine p75 molecules in a mouse T cell line. Int Immunol 1 (1989) 160-168
    • (1989) Int Immunol , vol.1 , pp. 160-168
    • Yamaguchi, A.1    Ide, T.2    Hatakeyama, M.3    Doi, T.4    Kono, T.5    Uchiyama, T.6
  • 70
    • 0026570314 scopus 로고
    • Evidence for p55-p75 heterodimers in the absence of IL-2 from Scatchard plot analysis
    • Goldstein B., Jones D., Kevrekidis I.G., and Perelson A.S. Evidence for p55-p75 heterodimers in the absence of IL-2 from Scatchard plot analysis. Int Immunol 4 (1992) 23-32
    • (1992) Int Immunol , vol.4 , pp. 23-32
    • Goldstein, B.1    Jones, D.2    Kevrekidis, I.G.3    Perelson, A.S.4
  • 71
    • 0028202442 scopus 로고
    • Cooperative interactions between the interleukin 2 receptor alpha and beta chains alter the interleukin 2-binding affinity of the receptor subunits
    • Roessler E., Grant A., Ju G., Tsudo M., Sugamura K., and Waldmann T.A. Cooperative interactions between the interleukin 2 receptor alpha and beta chains alter the interleukin 2-binding affinity of the receptor subunits. Proc Natl Acad Sci USA 91 (1994) 3344-3347
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3344-3347
    • Roessler, E.1    Grant, A.2    Ju, G.3    Tsudo, M.4    Sugamura, K.5    Waldmann, T.A.6
  • 72
    • 0027245994 scopus 로고
    • Unexpected effects of the IL-2 receptor alpha subunit on high affinity IL-2 receptor assembly and function detected with a mutant IL-2 analog
    • Kuziel W.A., Ju G., Grdina T.A., and Greene W.C. Unexpected effects of the IL-2 receptor alpha subunit on high affinity IL-2 receptor assembly and function detected with a mutant IL-2 analog. J Immunol 150 (1993) 3357-3365
    • (1993) J Immunol , vol.150 , pp. 3357-3365
    • Kuziel, W.A.1    Ju, G.2    Grdina, T.A.3    Greene, W.C.4
  • 73
    • 0026577201 scopus 로고
    • The interleukin 2 receptor (IL-2R): the IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit
    • Grant A.J., Roessler E., Ju G., Tsudo M., Sugamura K., and Waldmann T.A. The interleukin 2 receptor (IL-2R): the IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit. Proc Natl Acad Sci USA 89 (1992) 2165-2169
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2165-2169
    • Grant, A.J.1    Roessler, E.2    Ju, G.3    Tsudo, M.4    Sugamura, K.5    Waldmann, T.A.6
  • 74
    • 0025748606 scopus 로고
    • The IL-2 receptor alpha-chain alters the binding of IL-2 to the beta-chain
    • Arima N., Kamio M., Okuma M., Ju G., and Uchiyama T. The IL-2 receptor alpha-chain alters the binding of IL-2 to the beta-chain. J Immunol 147 (1991) 3396-3401
    • (1991) J Immunol , vol.147 , pp. 3396-3401
    • Arima, N.1    Kamio, M.2    Okuma, M.3    Ju, G.4    Uchiyama, T.5
  • 75
    • 0028832725 scopus 로고
    • Ligand binding kinetics of IL-2 and IL-15 to heteromers formed by extracellular domains of the three IL-2 receptor subunits
    • Balasubramanian S., Chernov-Rogan T., Davis A.M., Whitehorn E., Tate E., Bell M.P., et al. Ligand binding kinetics of IL-2 and IL-15 to heteromers formed by extracellular domains of the three IL-2 receptor subunits. Int Immunol 7 (1995) 1839-1849
    • (1995) Int Immunol , vol.7 , pp. 1839-1849
    • Balasubramanian, S.1    Chernov-Rogan, T.2    Davis, A.M.3    Whitehorn, E.4    Tate, E.5    Bell, M.P.6
  • 76
    • 0026521321 scopus 로고
    • An associated molecule, p64, with IL-2 receptor beta chain. Its possible involvement in the formation of the functional intermediate-affinity IL-2 receptor complex
    • Takeshita T., Ohtani K., Asao H., Kumaki S., Nakamura M., and Sugamura K. An associated molecule, p64, with IL-2 receptor beta chain. Its possible involvement in the formation of the functional intermediate-affinity IL-2 receptor complex. J Immunol 148 (1992) 2154-2158
    • (1992) J Immunol , vol.148 , pp. 2154-2158
    • Takeshita, T.1    Ohtani, K.2    Asao, H.3    Kumaki, S.4    Nakamura, M.5    Sugamura, K.6
  • 77
    • 0025298471 scopus 로고
    • An associated molecule, p64, with high-affinity interleukin 2 receptor
    • Takeshita T., Asao H., Suzuki J., and Sugamura K. An associated molecule, p64, with high-affinity interleukin 2 receptor. Int Immunol 2 (1990) 477-480
    • (1990) Int Immunol , vol.2 , pp. 477-480
    • Takeshita, T.1    Asao, H.2    Suzuki, J.3    Sugamura, K.4
  • 78
    • 0030695442 scopus 로고    scopus 로고
    • Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study
    • Damjanovich S., Bene L., Matkó J., Alileche A., Goldman C.K., Sharrow S., et al. Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study. Proc Natl Acad Sci USA 94 (1997) 13134-13139
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13134-13139
    • Damjanovich, S.1    Bene, L.2    Matkó, J.3    Alileche, A.4    Goldman, C.K.5    Sharrow, S.6
  • 80
    • 33645833872 scopus 로고    scopus 로고
    • The interleukin-15/interleukin-15 receptor system as a model for juxtacrine and reverse signaling
    • Bulfone-PauS S., Bulanova E., BudagianPaus V., and Paus R. The interleukin-15/interleukin-15 receptor system as a model for juxtacrine and reverse signaling. Bioessays 28 (2006) 362-377
    • (2006) Bioessays , vol.28 , pp. 362-377
    • Bulfone-PauS, S.1    Bulanova, E.2    BudagianPaus, V.3    Paus, R.4
  • 81
    • 29244436892 scopus 로고    scopus 로고
    • A promiscuous liaison between IL-15 receptor and Axl receptor tyrosine kinase in cell death control
    • Budagian V., Bulanova E., Orinska Z., Thon L., Mamat U., Bellosta P., et al. A promiscuous liaison between IL-15 receptor and Axl receptor tyrosine kinase in cell death control. EMBO J 24 (2005) 4260-4270
    • (2005) EMBO J , vol.24 , pp. 4260-4270
    • Budagian, V.1    Bulanova, E.2    Orinska, Z.3    Thon, L.4    Mamat, U.5    Bellosta, P.6
  • 82
    • 0034718756 scopus 로고    scopus 로고
    • IL-15/IL-15Ralpha intracellular trafficking in human melanoma cells and signal transduction through the IL-15Ralpha
    • Pereno R., Giron-Michel J., Gaggero A., Cazes E., Meazza R., Monetti M., et al. IL-15/IL-15Ralpha intracellular trafficking in human melanoma cells and signal transduction through the IL-15Ralpha. Oncogene 19 (2000) 5153-5162
    • (2000) Oncogene , vol.19 , pp. 5153-5162
    • Pereno, R.1    Giron-Michel, J.2    Gaggero, A.3    Cazes, E.4    Meazza, R.5    Monetti, M.6
  • 83
    • 3042826228 scopus 로고    scopus 로고
    • Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent mechanism: importance of the IL-15Ralpha chain
    • Ratthe C., and Girard D. Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent mechanism: importance of the IL-15Ralpha chain. J Leukoc Biol 76 (2004) 162-168
    • (2004) J Leukoc Biol , vol.76 , pp. 162-168
    • Ratthe, C.1    Girard, D.2
  • 84
    • 0035886940 scopus 로고    scopus 로고
    • T cell-independent interleukin 15Ralpha signals are required for bystander proliferation
    • Lodolce J.P., Burkett P.R., Boone D.L., Chien M., and Ma A. T cell-independent interleukin 15Ralpha signals are required for bystander proliferation. J Exp Med 194 (2001) 1187-1194
    • (2001) J Exp Med , vol.194 , pp. 1187-1194
    • Lodolce, J.P.1    Burkett, P.R.2    Boone, D.L.3    Chien, M.4    Ma, A.5
  • 85
    • 0037447075 scopus 로고    scopus 로고
    • IL-15R alpha expression on CD8+ T cells is dispensable for T cell memory
    • Burkett P.R., Koka R., Chien M., Chai S., Chan F., Ma A., et al. IL-15R alpha expression on CD8+ T cells is dispensable for T cell memory. Proc Natl Acad Sci USA 100 (2003) 4724-4729
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4724-4729
    • Burkett, P.R.1    Koka, R.2    Chien, M.3    Chai, S.4    Chan, F.5    Ma, A.6
  • 86
    • 0037460058 scopus 로고    scopus 로고
    • Interleukin (IL)-15R[alpha]-deficient natural killer cells survive in normal but not IL-15R[alpha]-deficient mice
    • Koka R., Burkett P.R., Chien M., Chai S., Chan F., Lodolce J.P., et al. Interleukin (IL)-15R[alpha]-deficient natural killer cells survive in normal but not IL-15R[alpha]-deficient mice. J Exp Med 197 (2003) 977-984
    • (2003) J Exp Med , vol.197 , pp. 977-984
    • Koka, R.1    Burkett, P.R.2    Chien, M.3    Chai, S.4    Chan, F.5    Lodolce, J.P.6
  • 87
    • 5444239242 scopus 로고    scopus 로고
    • Coordinate expression and trans presentation of interleukin (IL)-15Ralpha and IL-15 supports natural killer cell and memory CD8+ T cell homeostasis
    • Burkett P.R., Koka R., Chien M., Chai S., Boone D.L., and Ma A. Coordinate expression and trans presentation of interleukin (IL)-15Ralpha and IL-15 supports natural killer cell and memory CD8+ T cell homeostasis. J Exp Med 200 (2004) 825-834
    • (2004) J Exp Med , vol.200 , pp. 825-834
    • Burkett, P.R.1    Koka, R.2    Chien, M.3    Chai, S.4    Boone, D.L.5    Ma, A.6
  • 88
    • 4644288343 scopus 로고    scopus 로고
    • Cutting edge: murine dendritic cells require IL-15R alpha to prime NK cells
    • Koka R., Burkett P., Chien M., Chai S., Boone D.L., and Ma A. Cutting edge: murine dendritic cells require IL-15R alpha to prime NK cells. J Immunol 173 (2004) 3594-3598
    • (2004) J Immunol , vol.173 , pp. 3594-3598
    • Koka, R.1    Burkett, P.2    Chien, M.3    Chai, S.4    Boone, D.L.5    Ma, A.6
  • 89
    • 11244255868 scopus 로고    scopus 로고
    • Role of trans-cellular IL-15 presentation in the activation of NK cell-mediated killing, which leads to enhanced tumor immunosurveillance
    • Kobayashi H., Dubois S., Sato N., Sabzevari H., Sakai Y., Waldmann T.A., et al. Role of trans-cellular IL-15 presentation in the activation of NK cell-mediated killing, which leads to enhanced tumor immunosurveillance. Blood 105 (2005) 721-727
    • (2005) Blood , vol.105 , pp. 721-727
    • Kobayashi, H.1    Dubois, S.2    Sato, N.3    Sabzevari, H.4    Sakai, Y.5    Waldmann, T.A.6
  • 90
    • 9144241114 scopus 로고    scopus 로고
    • Cutting edge: transpresentation of IL-15 by bone marrow-derived cells necessitates expression of IL-15 and IL-15R alpha by the same cells
    • Sandau M.M., Schluns K.S., Lefrancois L., and Jameson S.C. Cutting edge: transpresentation of IL-15 by bone marrow-derived cells necessitates expression of IL-15 and IL-15R alpha by the same cells. J Immunol 173 (2004) 6537-6541
    • (2004) J Immunol , vol.173 , pp. 6537-6541
    • Sandau, M.M.1    Schluns, K.S.2    Lefrancois, L.3    Jameson, S.C.4
  • 91
    • 33846277906 scopus 로고    scopus 로고
    • The IL-15/IL-15Ralpha on cell surfaces enables sustained IL-15 activity and contributes to the long survival of CD8 memory T cells
    • Sato N., Patel H.J., Waldmann T.A., and Tagaya Y. The IL-15/IL-15Ralpha on cell surfaces enables sustained IL-15 activity and contributes to the long survival of CD8 memory T cells. Proc Natl Acad Sci USA 104 (2007) 588-593
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 588-593
    • Sato, N.1    Patel, H.J.2    Waldmann, T.A.3    Tagaya, Y.4
  • 92
    • 0032533796 scopus 로고    scopus 로고
    • IL-2R alpha on one cell can present IL-2 to IL-2R beta/gamma(c) on another cell to augment IL-2 signaling
    • Eicher D.M., and Waldmann T.A. IL-2R alpha on one cell can present IL-2 to IL-2R beta/gamma(c) on another cell to augment IL-2 signaling. J Immunol 161 (1998) 5430-5437
    • (1998) J Immunol , vol.161 , pp. 5430-5437
    • Eicher, D.M.1    Waldmann, T.A.2
  • 93
    • 40349110284 scopus 로고    scopus 로고
    • de Bakker BI, Bodnár A, van Dijk EMHP, Vámosi G, Damjanovich S, Waldmann TA, et al. Nanometer scale organization of the alpha subunits of interleukin-2 and -15 receptors (IL2Ralpha-IL15Ralpha) on Kit 225 FT7.10 human T lymphoma cells. J Cell Sci, in press.
    • de Bakker BI, Bodnár A, van Dijk EMHP, Vámosi G, Damjanovich S, Waldmann TA, et al. Nanometer scale organization of the alpha subunits of interleukin-2 and -15 receptors (IL2Ralpha-IL15Ralpha) on Kit 225 FT7.10 human T lymphoma cells. J Cell Sci, in press.
  • 95
    • 0038492661 scopus 로고    scopus 로고
    • Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model
    • Vereb G., Szöllo{combining double acute accent}si J., Matkó J., Nagy P., Farkas T., Vigh L., et al. Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model. Proc Natl Acad Sci USA 100 (2003) 8053-8058
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8053-8058
    • Vereb, G.1    Szöllosi, J.2    Matkó, J.3    Nagy, P.4    Farkas, T.5    Vigh, L.6
  • 96
    • 12944328730 scopus 로고    scopus 로고
    • Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts
    • Vereb G., Matkó J., Vámosi G., Ibrahim S.M., Magyar E., Varga S., et al. Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 97 (2000) 6013-6018
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6013-6018
    • Vereb, G.1    Matkó, J.2    Vámosi, G.3    Ibrahim, S.M.4    Magyar, E.5    Varga, S.6
  • 97
    • 18244402689 scopus 로고    scopus 로고
    • GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines
    • Matkó J., Bodnár A., Vereb G., Bene L., Vámosi G., Szentesi G., et al. GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines. Eur J Biochem 269 (2002) 1199-1208
    • (2002) Eur J Biochem , vol.269 , pp. 1199-1208
    • Matkó, J.1    Bodnár, A.2    Vereb, G.3    Bene, L.4    Vámosi, G.5    Szentesi, G.6
  • 98
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 99
    • 0037306407 scopus 로고    scopus 로고
    • The roles of membrane microdomains (rafts) in T cell activation
    • Horejsi V. The roles of membrane microdomains (rafts) in T cell activation. Immunol Rev 191 (2003) 148-164
    • (2003) Immunol Rev , vol.191 , pp. 148-164
    • Horejsi, V.1
  • 100
    • 0037013717 scopus 로고    scopus 로고
    • Landing of immune receptors and signal proteins on lipid rafts: a safe way to be spatio-temporally coordinated?
    • Matkó J., and Szöllo{combining double acute accent}si J. Landing of immune receptors and signal proteins on lipid rafts: a safe way to be spatio-temporally coordinated?. Immunol Lett 82 (2002) 3-15
    • (2002) Immunol Lett , vol.82 , pp. 3-15
    • Matkó, J.1    Szöllosi, J.2
  • 101
    • 0035469893 scopus 로고    scopus 로고
    • Role for lipid rafts in regulating interleukin-2 receptor signaling
    • Marmor M.D., and Julius M. Role for lipid rafts in regulating interleukin-2 receptor signaling. Blood 98 (2001) 1489-1497
    • (2001) Blood , vol.98 , pp. 1489-1497
    • Marmor, M.D.1    Julius, M.2
  • 102
    • 0036658748 scopus 로고    scopus 로고
    • Differential localization of IL-2- and -15 receptor chains in membrane rafts of human T cells
    • Goebel J., Forrest K., Morford L., and Roszman T.L. Differential localization of IL-2- and -15 receptor chains in membrane rafts of human T cells. J Leukoc Biol 72 (2002) 199-206
    • (2002) J Leukoc Biol , vol.72 , pp. 199-206
    • Goebel, J.1    Forrest, K.2    Morford, L.3    Roszman, T.L.4
  • 103
    • 33644663445 scopus 로고    scopus 로고
    • The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes
    • Vámosi G., Bodnár A., Damjanovich S., Nagy P., Varga Z., and Damjanovich L. The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes. Immunol Lett 104 (2006) 53-58
    • (2006) Immunol Lett , vol.104 , pp. 53-58
    • Vámosi, G.1    Bodnár, A.2    Damjanovich, S.3    Nagy, P.4    Varga, Z.5    Damjanovich, L.6
  • 104
    • 0028101424 scopus 로고
    • Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts: a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules
    • Bene L., Balazs M., Matkó J., Most J., Dierich M.P., Szöllo{combining double acute accent}si J., et al. Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts: a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules. Eur J Immunol 24 (1994) 2115-2123
    • (1994) Eur J Immunol , vol.24 , pp. 2115-2123
    • Bene, L.1    Balazs, M.2    Matkó, J.3    Most, J.4    Dierich, M.P.5    Szöllosi, J.6
  • 105
    • 0023433856 scopus 로고
    • Flow cytometric resonance energy transfer measurements support the association of a 95-kDa peptide termed T27 with the 55-kDa Tac peptide
    • Szöllo{combining double acute accent}si J., Damjanovich S., Goldman C.K., Fulwyler M.J., Aszalos A.A., Goldstein G., et al. Flow cytometric resonance energy transfer measurements support the association of a 95-kDa peptide termed T27 with the 55-kDa Tac peptide. Proc Natl Acad Sci USA 84 (1987) 7246-7250
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7246-7250
    • Szöllosi, J.1    Damjanovich, S.2    Goldman, C.K.3    Fulwyler, M.J.4    Aszalos, A.A.5    Goldstein, G.6
  • 106
    • 0023727232 scopus 로고
    • Lateral diffusion measurements give evidence for association of the Tac peptide of the IL-2 receptor with the T27 peptide in the plasma membrane of HUT-102-B2 T cells
    • Edidin M., Aszalos A., Damjanovich S., and Waldmann T.A. Lateral diffusion measurements give evidence for association of the Tac peptide of the IL-2 receptor with the T27 peptide in the plasma membrane of HUT-102-B2 T cells. J Immunol 141 (1988) 1206-1210
    • (1988) J Immunol , vol.141 , pp. 1206-1210
    • Edidin, M.1    Aszalos, A.2    Damjanovich, S.3    Waldmann, T.A.4
  • 107
    • 0023736047 scopus 로고
    • Possible association between IL-2 receptors and class I HLA molecules on T cells
    • Sharon M., Gnarra J.R., Baniyash M., and Leonard W.J. Possible association between IL-2 receptors and class I HLA molecules on T cells. J Immunol 141 (1988) 3512-3515
    • (1988) J Immunol , vol.141 , pp. 3512-3515
    • Sharon, M.1    Gnarra, J.R.2    Baniyash, M.3    Leonard, W.J.4
  • 108
    • 0035195023 scopus 로고    scopus 로고
    • Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors
    • Nagy P., Mátyus L., Jenei A., Panyi G., Varga S., Matkó J., et al. Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors. J Cell Sci 114 (2001) 4063-4071
    • (2001) J Cell Sci , vol.114 , pp. 4063-4071
    • Nagy, P.1    Mátyus, L.2    Jenei, A.3    Panyi, G.4    Varga, S.5    Matkó, J.6
  • 109
    • 0030700848 scopus 로고    scopus 로고
    • Interaction of class I human leukocyte antigen (HLA-I) molecules with insulin receptors and its effect on the insulin-signaling cascade
    • Ramalingam T.S., Chakrabarti A., and Edidin M. Interaction of class I human leukocyte antigen (HLA-I) molecules with insulin receptors and its effect on the insulin-signaling cascade. Mol Biol Cell 8 (1997) 2463-2474
    • (1997) Mol Biol Cell , vol.8 , pp. 2463-2474
    • Ramalingam, T.S.1    Chakrabarti, A.2    Edidin, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.