메뉴 건너뛰기




Volumn 224, Issue 1, 2008, Pages 249-264

Diacylglycerol kinases in immune cell function and self-tolerance

Author keywords

Diacylglycerol kinase; Mast cell; Phosphatidic acid; Signal transduction; T cell receptor; Toll like receptor

Indexed keywords

DIACYLGLYCEROL KINASE; IMMUNOGLOBULIN E; INTERLEUKIN 12; PHOSPHATIDIC ACID; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SUBUNIT; TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 49249109489     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2008.00647.x     Document Type: Review
Times cited : (80)

References (173)
  • 3
    • 38149018650 scopus 로고    scopus 로고
    • Diacylglycerol kinases: At the hub of cell signalling
    • Merida I, Avila-Flores A, Merino E. Diacylglycerol kinases: at the hub of cell signalling. Biochem J 2008 409 : 1 18.
    • (2008) Biochem J , vol.409 , pp. 1-18
    • Merida, I.1    Avila-Flores, A.2    Merino, E.3
  • 4
    • 0037705412 scopus 로고    scopus 로고
    • Synthesis and phorbol ester binding of the cysteine-rich domains of diacylglycerol kinase (DGK) isozymes. DGKα and DGKβ are new targets of tumor-promoting phorbol esters
    • Shindo M, et al. Synthesis and phorbol ester binding of the cysteine-rich domains of diacylglycerol kinase (DGK) isozymes. DGKα and DGKβ are new targets of tumor-promoting phorbol esters. J Biol Chem 2003 278 : 18448 18454.
    • (2003) J Biol Chem , vol.278 , pp. 18448-18454
    • Shindo, M.1
  • 5
    • 0029792364 scopus 로고    scopus 로고
    • The C-terminal part of diacylglycerol kinase α lacking zinc fingers serves as a catalytic domain
    • Sakane F, Kai M, Wada I, Imai S, Kanoh H. The C-terminal part of diacylglycerol kinase α lacking zinc fingers serves as a catalytic domain. Biochem J 1996 318 : 583 590.
    • (1996) Biochem J , vol.318 , pp. 583-590
    • Sakane, F.1    Kai, M.2    Wada, I.3    Imai, S.4    Kanoh, H.5
  • 6
    • 36849005359 scopus 로고    scopus 로고
    • Role of the diacylglycerol kinase α-conserved domains in membrane targeting in intact T cells
    • Merino E, Sanjuan MA, Moraga I, Cipres A, Merida I. Role of the diacylglycerol kinase α-conserved domains in membrane targeting in intact T cells. J Biol Chem 2007 282 : 35396 35404.
    • (2007) J Biol Chem , vol.282 , pp. 35396-35404
    • Merino, E.1    Sanjuan, M.A.2    Moraga, I.3    Cipres, A.4    Merida, I.5
  • 7
    • 27144526243 scopus 로고    scopus 로고
    • Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases (DGKs), displays unique biochemical features and saturates at low substrate concentration: The DGK inhibitor R59022 differentially affects AtDGK2 and AtDGK7 activity in vitro and alters plant growth and development
    • Gomez-Merino FC, et al. Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases (DGKs), displays unique biochemical features and saturates at low substrate concentration: the DGK inhibitor R59022 differentially affects AtDGK2 and AtDGK7 activity in vitro and alters plant growth and development. J Biol Chem 2005 280 : 34888 34899.
    • (2005) J Biol Chem , vol.280 , pp. 34888-34899
    • Gomez-Merino, F.C.1
  • 8
    • 1542349817 scopus 로고    scopus 로고
    • AtDGK2, a novel diacylglycerol kinase from Arabidopsis thaliana, phosphorylates 1-stearoyl-2-arachidonoyl-sn-glycerol and 1,2-dioleoyl-sn- glycerol and exhibits cold-inducible gene expression
    • Gomez-Merino FC, Brearley CA, Ornatowska M, Abdel-Haliem ME, Zanor MI, Mueller-Roeber B. AtDGK2, a novel diacylglycerol kinase from Arabidopsis thaliana, phosphorylates 1-stearoyl-2-arachidonoyl-sn-glycerol and 1,2-dioleoyl-sn-glycerol and exhibits cold-inducible gene expression. J Biol Chem 2004 279 : 8230 8241.
    • (2004) J Biol Chem , vol.279 , pp. 8230-8241
    • Gomez-Merino, F.C.1    Brearley, C.A.2    Ornatowska, M.3    Abdel-Haliem, M.E.4    Zanor, M.I.5    Mueller-Roeber, B.6
  • 9
    • 0037119466 scopus 로고    scopus 로고
    • Dynamics of diacylglycerol kinase ζ translocation in living T-cells. Study of the structural domain requirements for translocation and activity
    • Santos T, Carrasco S, Jones DR, Merida I, Eguinoa A. Dynamics of diacylglycerol kinase ζ translocation in living T-cells. Study of the structural domain requirements for translocation and activity. J Biol Chem 2002 277 : 30300 30309.
    • (2002) J Biol Chem , vol.277 , pp. 30300-30309
    • Santos, T.1    Carrasco, S.2    Jones, D.R.3    Merida, I.4    Eguinoa, A.5
  • 10
    • 15444373874 scopus 로고    scopus 로고
    • Translocation of diacylglycerol kinase θ from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C
    • van Baal J, de Widt J, Divecha N, van Blitterswijk WJ. Translocation of diacylglycerol kinase θ from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C. J Biol Chem 2005 280 : 9870 9878.
    • (2005) J Biol Chem , vol.280 , pp. 9870-9878
    • Van Baal, J.1    De Widt, J.2    Divecha, N.3    Van Blitterswijk, W.J.4
  • 11
    • 0034637434 scopus 로고    scopus 로고
    • Subtype-specific translocation of diacylglycerol kinase α and γ and its correlation with protein kinase C
    • Shirai Y, Segawa S, Kuriyama M, Goto K, Sakai N, Saito N. Subtype-specific translocation of diacylglycerol kinase α and γ and its correlation with protein kinase C. J Biol Chem 2000 275 : 24760 24766.
    • (2000) J Biol Chem , vol.275 , pp. 24760-24766
    • Shirai, Y.1    Segawa, S.2    Kuriyama, M.3    Goto, K.4    Sakai, N.5    Saito, N.6
  • 12
    • 0042817949 scopus 로고    scopus 로고
    • Regulation of diacylglycerol kinase α by phosphoinositide 3-kinase lipid products
    • Cipres A, et al. Regulation of diacylglycerol kinase α by phosphoinositide 3-kinase lipid products. J Biol Chem 2003 278 : 35629 35635.
    • (2003) J Biol Chem , vol.278 , pp. 35629-35635
    • Cipres, A.1
  • 14
    • 0025270758 scopus 로고
    • Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs
    • Sakane F, Yamada K, Kanoh H, Yokoyama C, Tanabe T. Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Nature 1990 344 : 345 348.
    • (1990) Nature , vol.344 , pp. 345-348
    • Sakane, F.1    Yamada, K.2    Kanoh, H.3    Yokoyama, C.4    Tanabe, T.5
  • 15
    • 0025008451 scopus 로고
    • Purification, cDNA-cloning and expression of human diacylglycerol kinase
    • Schaap D, et al. Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett 1990 275 : 151 158.
    • (1990) FEBS Lett , vol.275 , pp. 151-158
    • Schaap, D.1
  • 16
    • 0027257457 scopus 로고
    • Molecular cloning and expression of a 90-kDa diacylglycerol kinase that predominantly localizes in neurons
    • Goto K, Kondo H. Molecular cloning and expression of a 90-kDa diacylglycerol kinase that predominantly localizes in neurons. Proc Natl Acad Sci USA 1993 90 : 7598 7602.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7598-7602
    • Goto, K.1    Kondo, H.2
  • 17
    • 0028598685 scopus 로고
    • Cloning and expression of a cytoskeleton-associated diacylglycerol kinase that is dominantly expressed in cerebellum
    • Goto K, Funayama M, Kondo H. Cloning and expression of a cytoskeleton-associated diacylglycerol kinase that is dominantly expressed in cerebellum. Proc Natl Acad Sci USA 1994 91 : 13042 13046.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 13042-13046
    • Goto, K.1    Funayama, M.2    Kondo, H.3
  • 18
    • 0034602168 scopus 로고    scopus 로고
    • A domain with homology to neuronal calcium sensors is required for calcium-dependent activation of diacylglycerol kinase α
    • Jiang Y, Qian W, Hawes JW, Walsh JP. A domain with homology to neuronal calcium sensors is required for calcium-dependent activation of diacylglycerol kinase α. J Biol Chem 2000 275 : 34092 34099.
    • (2000) J Biol Chem , vol.275 , pp. 34092-34099
    • Jiang, Y.1    Qian, W.2    Hawes, J.W.3    Walsh, J.P.4
  • 19
    • 0029877466 scopus 로고    scopus 로고
    • Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases
    • Sakane F, Imai S, Kai M, Wada I, Kanoh H. Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem 1996 271 : 8394 8401.
    • (1996) J Biol Chem , vol.271 , pp. 8394-8401
    • Sakane, F.1    Imai, S.2    Kai, M.3    Wada, I.4    Kanoh, H.5
  • 20
    • 0029811987 scopus 로고    scopus 로고
    • Cloning and characterization of a glucocorticoid-induced diacylglycerol kinase
    • Klauck TM, Xu X, Mousseau B, Jaken S. Cloning and characterization of a glucocorticoid-induced diacylglycerol kinase. J Biol Chem 1996 271 : 19781 19788.
    • (1996) J Biol Chem , vol.271 , pp. 19781-19788
    • Klauck, T.M.1    Xu, X.2    Mousseau, B.3    Jaken, S.4
  • 21
    • 28844495301 scopus 로고    scopus 로고
    • Identification and characterization of a novel human type II diacylglycerol kinase, DGKκ
    • Imai S-i, Kai M, Yasuda S, Kanoh H, Sakane F. Identification and characterization of a novel human type II diacylglycerol kinase, DGKκ. J Biol Chem 2005 280 : 39870 39881.
    • (2005) J Biol Chem , vol.280 , pp. 39870-39881
    • Imai, S.-I.1    Kai, M.2    Yasuda, S.3    Kanoh, H.4    Sakane, F.5
  • 22
    • 0037144417 scopus 로고    scopus 로고
    • Phorbol ester-regulated oligomerization of diacylglycerol kinase δ linked to its phosphorylation and translocation
    • Imai S, Sakane F, Kanoh H. Phorbol ester-regulated oligomerization of diacylglycerol kinase δ linked to its phosphorylation and translocation. J Biol Chem 2002 277 : 35323 35332.
    • (2002) J Biol Chem , vol.277 , pp. 35323-35332
    • Imai, S.1    Sakane, F.2    Kanoh, H.3
  • 23
    • 4744364185 scopus 로고    scopus 로고
    • The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain
    • Imai S, Kai M, Yamada K, Kanoh H, Sakane F. The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain. Biochem J 2004 382 : 957 966.
    • (2004) Biochem J , vol.382 , pp. 957-966
    • Imai, S.1    Kai, M.2    Yamada, K.3    Kanoh, H.4    Sakane, F.5
  • 24
    • 0036151633 scopus 로고    scopus 로고
    • Diacylglycerol kinase δ suppresses ER-to-Golgi traffic via its SAM and PH domains
    • Nagaya H, Wada I, Jia YJ, Kanoh H. Diacylglycerol kinase δ suppresses ER-to-Golgi traffic via its SAM and PH domains. Mol Biol Cell 2002 13 : 302 316.
    • (2002) Mol Biol Cell , vol.13 , pp. 302-316
    • Nagaya, H.1    Wada, I.2    Jia, Y.J.3    Kanoh, H.4
  • 25
    • 0029937610 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel human diacylglycerol kinase ζ
    • Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM. Molecular cloning and characterization of a novel human diacylglycerol kinase ζ. J Biol Chem 1996 271 : 10230 10236.
    • (1996) J Biol Chem , vol.271 , pp. 10230-10236
    • Bunting, M.1    Tang, W.2    Zimmerman, G.A.3    McIntyre, T.M.4    Prescott, S.M.5
  • 26
    • 0029784474 scopus 로고    scopus 로고
    • A 104-kDa diacylglycerol kinase containing ankyrin-like repeats localizes in the cell nucleus
    • Goto K, Kondo H. A 104-kDa diacylglycerol kinase containing ankyrin-like repeats localizes in the cell nucleus. Proc Natl Acad Sci USA 1996 93 : 11196 11201.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11196-11201
    • Goto, K.1    Kondo, H.2
  • 27
    • 0032484120 scopus 로고    scopus 로고
    • The cloning and characterization of a novel human diacylglycerol kinase, DGKι
    • Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM. The cloning and characterization of a novel human diacylglycerol kinase, DGKι. J Biol Chem 1998 273 : 32746 32752.
    • (1998) J Biol Chem , vol.273 , pp. 32746-32752
    • Ding, L.1    Traer, E.2    McIntyre, T.M.3    Zimmerman, G.A.4    Prescott, S.M.5
  • 29
    • 34250320543 scopus 로고    scopus 로고
    • Morphological changes and spatial regulation of diacylglycerol kinase ζ, syntrophins, and Rac1 during myoblast fusion
    • Abramovici H, Gee SH. Morphological changes and spatial regulation of diacylglycerol kinase ζ, syntrophins, and Rac1 during myoblast fusion. Cell Motil Cytoskeleton 2007 64 : 549 567.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 549-567
    • Abramovici, H.1    Gee, S.H.2
  • 30
    • 0345687302 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins
    • Abramovici H, Hogan AB, Obagi C, Topham MK, Gee SH. Diacylglycerol kinase ζ localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins. Mol Biol Cell 2003 14 : 4499 4511.
    • (2003) Mol Biol Cell , vol.14 , pp. 4499-4511
    • Abramovici, H.1    Hogan, A.B.2    Obagi, C.3    Topham, M.K.4    Gee, S.H.5
  • 31
    • 0035854664 scopus 로고    scopus 로고
    • Interaction of γ1-syntrophin with diacylglycerol kinase ζ. Regulation of nuclear localization by PDZ interactions
    • Hogan A, et al. Interaction of γ1-syntrophin with diacylglycerol kinase ζ. Regulation of nuclear localization by PDZ interactions. J Biol Chem 2001 276 : 26526 26533.
    • (2001) J Biol Chem , vol.276 , pp. 26526-26533
    • Hogan, A.1
  • 32
    • 0030889241 scopus 로고    scopus 로고
    • Cloning of a novel human diacylglycerol kinase (DGKθ) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain
    • Houssa B, et al. Cloning of a novel human diacylglycerol kinase (DGKθ) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain. J Biol Chem 1997 272 : 10422 10428.
    • (1997) J Biol Chem , vol.272 , pp. 10422-10428
    • Houssa, B.1
  • 34
    • 0037443550 scopus 로고    scopus 로고
    • T cell activation in vivo targets diacylglycerol Kinase α to the membrane: A novel mechanism for Ras attenuation
    • Sanjuan MA, et al. T cell activation in vivo targets diacylglycerol Kinase α to the membrane: a novel mechanism for Ras attenuation. J Immunol 2003 170 : 2877 2883.
    • (2003) J Immunol , vol.170 , pp. 2877-2883
    • Sanjuan, M.A.1
  • 35
    • 0037163130 scopus 로고    scopus 로고
    • Regulation of T cell receptor-induced activation of the Ras-Erk pathway by diacylglycerol kinase ζ
    • Zhong XP, Hainey EA, Olenchock BA, Zhao H, Topham MK, Koretzky GA. Regulation of T cell receptor-induced activation of the Ras-Erk pathway by diacylglycerol kinase ζ. J Biol Chem 2002 277 : 31089 31098.
    • (2002) J Biol Chem , vol.277 , pp. 31089-31098
    • Zhong, X.P.1    Hainey, E.A.2    Olenchock, B.A.3    Zhao, H.4    Topham, M.K.5    Koretzky, G.A.6
  • 36
    • 33750094147 scopus 로고    scopus 로고
    • Disruption of diacylglycerol metabolism impairs the induction of T cell anergy
    • Olenchock BA, et al. Disruption of diacylglycerol metabolism impairs the induction of T cell anergy. Nat Immunol 2006 7 : 1174 1181.
    • (2006) Nat Immunol , vol.7 , pp. 1174-1181
    • Olenchock, B.A.1
  • 37
    • 0029998639 scopus 로고    scopus 로고
    • Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates
    • Tang W, Bunting M, Zimmerman GA, McIntyre TM, Prescott SM. Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates. J Biol Chem 1996 271 : 10237 10241.
    • (1996) J Biol Chem , vol.271 , pp. 10237-10241
    • Tang, W.1    Bunting, M.2    Zimmerman, G.A.3    McIntyre, T.M.4    Prescott, S.M.5
  • 38
    • 0032080795 scopus 로고    scopus 로고
    • Glucosylceramide synthase and glycosphingolipid synthesis
    • Ichikawa S, Hirabayashi Y. Glucosylceramide synthase and glycosphingolipid synthesis. Trends Cell Biol 1998 8 : 198 202.
    • (1998) Trends Cell Biol , vol.8 , pp. 198-202
    • Ichikawa, S.1    Hirabayashi, Y.2
  • 39
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • Griner EM, Kazanietz MG. Protein kinase C and other diacylglycerol effectors in cancer. Nat Rev Cancer 2007 7 : 281 294.
    • (2007) Nat Rev Cancer , vol.7 , pp. 281-294
    • Griner, E.M.1    Kazanietz, M.G.2
  • 40
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I, Rosenmund C, Sudhof TC, Brose N. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 1999 400 : 457 461.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Sudhof, T.C.3    Brose, N.4
  • 41
    • 18244389735 scopus 로고    scopus 로고
    • β phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs
    • Rhee JS, et al. β phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs. Cell 2002 108 : 121 133.
    • (2002) Cell , vol.108 , pp. 121-133
    • Rhee, J.S.1
  • 42
    • 0032589433 scopus 로고    scopus 로고
    • β2-chimaerin is a novel target for diacylglycerol: Binding properties and changes in subcellular localization mediated by ligand binding to its C1 domain
    • Caloca MJ, et al. β2-chimaerin is a novel target for diacylglycerol: binding properties and changes in subcellular localization mediated by ligand binding to its C1 domain. Proc Natl Acad Sci USA 1999 96 : 11854 11859.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11854-11859
    • Caloca, M.J.1
  • 44
    • 0033554368 scopus 로고    scopus 로고
    • Binding of phosphatidic acid to the protein-tyrosine phosphatase SHP-1 as a basis for activity modulation
    • Frank C, Keilhack H, Opitz F, Zschornig O, Bohmer FD. Binding of phosphatidic acid to the protein-tyrosine phosphatase SHP-1 as a basis for activity modulation. Biochemistry 1999 38 : 11993 12002.
    • (1999) Biochemistry , vol.38 , pp. 11993-12002
    • Frank, C.1    Keilhack, H.2    Opitz, F.3    Zschornig, O.4    Bohmer, F.D.5
  • 45
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y, Vilella-Bach M, Bachmann R, Flanigan A, Chen J. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 2001 294 : 1942 1945.
    • (2001) Science , vol.294 , pp. 1942-1945
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 46
    • 0037013237 scopus 로고    scopus 로고
    • Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid
    • Jones JA, Hannun YA. Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid. J Biol Chem 2002 277 : 15530 15538.
    • (2002) J Biol Chem , vol.277 , pp. 15530-15538
    • Jones, J.A.1    Hannun, Y.A.2
  • 47
    • 33845658111 scopus 로고    scopus 로고
    • Phosphatidic acid regulates the affinity of the murine phosphatidylinositol 4-phosphate 5-kinase-Iβ for phosphatidylinositol-4- phosphate
    • Jarquin-Pardo M, Fitzpatrick A, Galiano FJ, First EA, Davis JN. Phosphatidic acid regulates the affinity of the murine phosphatidylinositol 4-phosphate 5-kinase-Iβ for phosphatidylinositol-4-phosphate. J Cell Biochem 2007 100 : 112 128.
    • (2007) J Cell Biochem , vol.100 , pp. 112-128
    • Jarquin-Pardo, M.1    Fitzpatrick, A.2    Galiano, F.J.3    First, E.A.4    Davis, J.N.5
  • 48
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins GH, Fisette PL, Anderson RA. Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J Biol Chem 1994 269 : 11547 11554.
    • (1994) J Biol Chem , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 49
    • 0026744154 scopus 로고
    • Phosphatidic acid is a specific activator of phosphatidylinositol-4- phosphate kinase
    • Moritz A, De Graan PN, Gispen WH, Wirtz KW. Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase. J Biol Chem 1992 267 : 7207 7210.
    • (1992) J Biol Chem , vol.267 , pp. 7207-7210
    • Moritz, A.1    De Graan, P.N.2    Gispen, W.H.3    Wirtz, K.W.4
  • 50
    • 0026322028 scopus 로고
    • Ras GTPase-activating protein physically associates with mitogenically active phospholipids
    • Tsai MH, Roudebush M, Dobrowolski S, Yu CL, Gibbs JB, Stacey DW. Ras GTPase-activating protein physically associates with mitogenically active phospholipids. Mol Cell Biol 1991 11 : 2785 2793.
    • (1991) Mol Cell Biol , vol.11 , pp. 2785-2793
    • Tsai, M.H.1    Roudebush, M.2    Dobrowolski, S.3    Yu, C.L.4    Gibbs, J.B.5    Stacey, D.W.6
  • 51
    • 0242664746 scopus 로고    scopus 로고
    • Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: Mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos
    • Ghosh S, Moore S, Bell RM, Dush M. Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos. J Biol Chem 2003 278 : 45690 45696.
    • (2003) J Biol Chem , vol.278 , pp. 45690-45696
    • Ghosh, S.1    Moore, S.2    Bell, R.M.3    Dush, M.4
  • 52
    • 0036791737 scopus 로고    scopus 로고
    • phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. Embo J 2002 21 : 5057 5068.
    • (2002) Embo J , vol.21 , pp. 5057-5068
    • Karathanassis, D.1
  • 53
    • 34447568476 scopus 로고    scopus 로고
    • Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos
    • Zhao C, Du G, Skowronek K, Frohman MA, Bar-Sagi D. Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nat Cell Biol 2007 9 : 706 712.
    • (2007) Nat Cell Biol , vol.9 , pp. 706-712
    • Zhao, C.1    Du, G.2    Skowronek, K.3    Frohman, M.A.4    Bar-Sagi, D.5
  • 54
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
    • Tsui HW, Siminovitch KA, de Souza L, Tsui FW. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat Genet 1993 4 : 124 129.
    • (1993) Nat Genet , vol.4 , pp. 124-129
    • Tsui, H.W.1    Siminovitch, K.A.2    De Souza, L.3    Tsui, F.W.4
  • 55
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N. Upstream and downstream of mTOR. Genes Dev 2004 18 : 1926 1945.
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 57
    • 2442602613 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ regulates phosphatidylinositol 4-phosphate 5-kinase Iα by a novel mechanism
    • Luo B, Prescott SM, Topham MK. Diacylglycerol kinase ζ regulates phosphatidylinositol 4-phosphate 5-kinase Iα by a novel mechanism. Cell Signal 2004 16 : 891 897.
    • (2004) Cell Signal , vol.16 , pp. 891-897
    • Luo, B.1    Prescott, S.M.2    Topham, M.K.3
  • 58
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • Avila-Flores A, Santos T, Rincon E, Merida I. Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid. J Biol Chem 2005 280 : 10091 10099.
    • (2005) J Biol Chem , vol.280 , pp. 10091-10099
    • Avila-Flores, A.1    Santos, T.2    Rincon, E.3    Merida, I.4
  • 59
    • 34247401626 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ regulates microbial recognition and host resistance to Toxoplasma gondii
    • Liu CH, et al. Diacylglycerol kinase ζ regulates microbial recognition and host resistance to Toxoplasma gondii. J Exp Med 2007 204 : 781 792.
    • (2007) J Exp Med , vol.204 , pp. 781-792
    • Liu, C.H.1
  • 60
    • 0033565429 scopus 로고    scopus 로고
    • Diacylglycerol kinase inhibition prevents IL-2-induced G1 to S transition through a phosphatidylinositol-3 kinase-independent mechanism
    • Flores I, Jones DR, Cipres A, Diaz-Flores E, Sanjuan MA, Merida I. Diacylglycerol kinase inhibition prevents IL-2-induced G1 to S transition through a phosphatidylinositol-3 kinase-independent mechanism. J Immunol 1999 163 : 708 714.
    • (1999) J Immunol , vol.163 , pp. 708-714
    • Flores, I.1    Jones, D.R.2    Cipres, A.3    Diaz-Flores, E.4    Sanjuan, M.A.5    Merida, I.6
  • 61
    • 0034282538 scopus 로고    scopus 로고
    • Src-mediated activation of α-diacylglycerol kinase is required for hepatocyte growth factor-induced cell motility
    • Cutrupi S, et al. Src-mediated activation of α-diacylglycerol kinase is required for hepatocyte growth factor-induced cell motility. EMBO J 2000 19 : 4614 4622.
    • (2000) EMBO J , vol.19 , pp. 4614-4622
    • Cutrupi, S.1
  • 62
    • 34047177038 scopus 로고    scopus 로고
    • Diacylglycerol kinase α suppresses tumor necrosis factor-α-induced apoptosis of human melanoma cells through NF-κB activation
    • Yanagisawa K, et al. Diacylglycerol kinase α suppresses tumor necrosis factor-α-induced apoptosis of human melanoma cells through NF-κB activation. Biochim Biophys Acta 2007 1771 : 462 474.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 462-474
    • Yanagisawa, K.1
  • 63
    • 24744438265 scopus 로고    scopus 로고
    • Activation of α-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase
    • Bacchiocchi R, et al. Activation of α-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase. Blood 2005 106 : 2175 2182.
    • (2005) Blood , vol.106 , pp. 2175-2182
    • Bacchiocchi, R.1
  • 64
    • 4644288370 scopus 로고    scopus 로고
    • Superoxide production at phagosomal cup/phagosome through βi protein kinase C during FcγR-mediated phagocytosis in microglia
    • Ueyama T, et al. Superoxide production at phagosomal cup/phagosome through βI protein kinase C during FcγR-mediated phagocytosis in microglia. J Immunol 2004 173 : 4582 4589.
    • (2004) J Immunol , vol.173 , pp. 4582-4589
    • Ueyama, T.1
  • 65
    • 3142616908 scopus 로고    scopus 로고
    • Diacylglycerol kinase γ serves as an upstream suppressor of Rac1 and lamellipodium formation
    • Tsushima S, et al. Diacylglycerol kinase γ serves as an upstream suppressor of Rac1 and lamellipodium formation. J Biol Chem 2004 279 : 28603 28613.
    • (2004) J Biol Chem , vol.279 , pp. 28603-28613
    • Tsushima, S.1
  • 66
    • 33846444740 scopus 로고    scopus 로고
    • Diacylglycerol kinase γ interacts with and activates β2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor
    • Yasuda S, Kai M, Imai S, Kanoh H, Sakane F. Diacylglycerol kinase γ interacts with and activates β2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor. FEBS Lett 2007 581 : 551 557.
    • (2007) FEBS Lett , vol.581 , pp. 551-557
    • Yasuda, S.1    Kai, M.2    Imai, S.3    Kanoh, H.4    Sakane, F.5
  • 67
    • 38149086943 scopus 로고    scopus 로고
    • Phorbol ester and hydrogen peroxide synergistically induce the interaction of diacylglycerol kinase γ with the Src homology 2 and C1 domains of β2-chimaerin
    • Yasuda S, Kai M, Imai S, Kanoh H, Sakane F. Phorbol ester and hydrogen peroxide synergistically induce the interaction of diacylglycerol kinase γ with the Src homology 2 and C1 domains of β2-chimaerin. Biochem J 2008 409 : 95 106.
    • (2008) Biochem J , vol.409 , pp. 95-106
    • Yasuda, S.1    Kai, M.2    Imai, S.3    Kanoh, H.4    Sakane, F.5
  • 68
    • 33750334731 scopus 로고    scopus 로고
    • Diacylglycerol kinase δ regulates protein kinase C and epidermal growth factor receptor signaling
    • Crotty T, Cai J, Sakane F, Taketomi A, Prescott SM, Topham MK. Diacylglycerol kinase δ regulates protein kinase C and epidermal growth factor receptor signaling. Proc Natl Acad Sci USA 2006 103 : 15485 15490.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15485-15490
    • Crotty, T.1    Cai, J.2    Sakane, F.3    Taketomi, A.4    Prescott, S.M.5    Topham, M.K.6
  • 69
    • 38749110035 scopus 로고    scopus 로고
    • Regulation of clathrin-dependent endocytosis by diacylglycerol kinase δ: iiimportance of kinase activity and binding to AαP2
    • Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N. Regulation of clathrin-dependent endocytosis by diacylglycerol kinase δ: importance of kinase activity and binding to AP2α. Biochem J 2008 409 : 471 479.
    • (2008) Biochem J , vol.409 , pp. 471-479
    • Kawasaki, T.1    Kobayashi, T.2    Ueyama, T.3    Shirai, Y.4    Saito, N.5
  • 70
    • 0035836345 scopus 로고    scopus 로고
    • Diacylglycerol kinase epsilon regulates seizure susceptibility and long-term potentiation through arachidonoyl- inositol lipid signaling
    • Rodriguez de Turco EB, et al. Diacylglycerol kinase epsilon regulates seizure susceptibility and long-term potentiation through arachidonoyl- inositol lipid signaling. Proc Natl Acad Sci USA 2001 98 : 4740 4745.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4740-4745
    • Rodriguez De Turco, E.B.1
  • 71
    • 33645310932 scopus 로고    scopus 로고
    • Diacylglycerol kinase ε modulates rapid kindling epileptogenesis
    • Musto A, Bazan NG. Diacylglycerol kinase ε modulates rapid kindling epileptogenesis. Epilepsia 2006 47 : 267 276.
    • (2006) Epilepsia , vol.47 , pp. 267-276
    • Musto, A.1    Bazan, N.G.2
  • 72
    • 1642564476 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone-induced activation of diacylglycerol kinase-ζ and its association with active c-Src
    • Davidson L, et al. Gonadotropin-releasing hormone-induced activation of diacylglycerol kinase-ζ and its association with active c-Src. J Biol Chem 2004 279 : 11906 11916.
    • (2004) J Biol Chem , vol.279 , pp. 11906-11916
    • Davidson, L.1
  • 73
    • 33846598517 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ attenuates pressure overload-induced cardiac hypertrophy
    • Harada M, et al. Diacylglycerol kinase ζ attenuates pressure overload-induced cardiac hypertrophy. Circ J 2007 71 : 276 282.
    • (2007) Circ J , vol.71 , pp. 276-282
    • Harada, M.1
  • 74
    • 33644867893 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of diacylglycerol kinase ζ prevents Gq protein-coupled receptor agonist-induced cardiac hypertrophy in transgenic mice
    • Arimoto T, et al. Cardiac-specific overexpression of diacylglycerol kinase ζ prevents Gq protein-coupled receptor agonist-induced cardiac hypertrophy in transgenic mice. Circulation 2006 113 : 60 66.
    • (2006) Circulation , vol.113 , pp. 60-66
    • Arimoto, T.1
  • 76
    • 33646539193 scopus 로고    scopus 로고
    • Nuclear transportation of diacylglycerol kinase γ and its possible function in the nucleus
    • Matsubara T, et al. Nuclear transportation of diacylglycerol kinase γ and its possible function in the nucleus. J Biol Chem 2006 281 : 6152 6164.
    • (2006) J Biol Chem , vol.281 , pp. 6152-6164
    • Matsubara, T.1
  • 77
    • 33745043950 scopus 로고    scopus 로고
    • Impaired degranulation but enhanced cytokine production after FcεRI stimulation of diacylglycerol kinase ζ-deficient mast cells
    • Olenchock BA, et al. Impaired degranulation but enhanced cytokine production after FcεRI stimulation of diacylglycerol kinase ζ-deficient mast cells. J Exp Med 2006 203 : 1471 1480.
    • (2006) J Exp Med , vol.203 , pp. 1471-1480
    • Olenchock, B.A.1
  • 78
    • 35248861267 scopus 로고    scopus 로고
    • Nuclear diacylglycerol kinase-ζ is a negative regulator of cell cycle progression in C2C12 mouse myoblasts
    • Evangelisti C, et al. Nuclear diacylglycerol kinase-ζ is a negative regulator of cell cycle progression in C2C12 mouse myoblasts. FASEB J 2007 22 : 3297 3307.
    • (2007) FASEB J , vol.22 , pp. 3297-3307
    • Evangelisti, C.1
  • 79
    • 0042383362 scopus 로고    scopus 로고
    • Enhanced T cell responses due to diacylglycerol kinase ζ deficiency
    • Zhong XP, et al. Enhanced T cell responses due to diacylglycerol kinase ζ deficiency. Nat Immunol 2003 4 : 882 890.
    • (2003) Nat Immunol , vol.4 , pp. 882-890
    • Zhong, X.P.1
  • 80
    • 33750093594 scopus 로고    scopus 로고
    • T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α
    • Zha Y, et al. T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α. Nat Immunol 2006 7 : 1166 1173.
    • (2006) Nat Immunol , vol.7 , pp. 1166-1173
    • Zha, Y.1
  • 81
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998 92 : 83 92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 82
    • 0000082758 scopus 로고    scopus 로고
    • Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function
    • Wardenburg JB, et al. Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function. J Biol Chem 1996 271 : 19641 19644.
    • (1996) J Biol Chem , vol.271 , pp. 19641-19644
    • Wardenburg, J.B.1
  • 83
    • 0030002904 scopus 로고    scopus 로고
    • Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production
    • Motto DG, Ross SE, Wu J, Hendricks-Taylor LR, Koretzky GA. Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. J Exp Med 1996 183 : 1937 1943.
    • (1996) J Exp Med , vol.183 , pp. 1937-1943
    • Motto, D.G.1    Ross, S.E.2    Wu, J.3    Hendricks-Taylor, L.R.4    Koretzky, G.A.5
  • 84
    • 0035525572 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation by adaptor proteins
    • Koretzky GA, Myung PS. Positive and negative regulation of T-cell activation by adaptor proteins. Nat Rev Immunol 2001 1 : 95 107.
    • (2001) Nat Rev Immunol , vol.1 , pp. 95-107
    • Koretzky, G.A.1    Myung, P.S.2
  • 85
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • Kane LP, Lin J, Weiss A. Signal transduction by the TCR for antigen. Curr Opin Immunol 2000 12 : 242 249.
    • (2000) Curr Opin Immunol , vol.12 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 86
    • 0034644505 scopus 로고    scopus 로고
    • Signaling takes shape in the immune system
    • Dustin ML, Chan AC. Signaling takes shape in the immune system. Cell 2000 103 : 283 294.
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.L.1    Chan, A.C.2
  • 87
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-γ1 in an SLP-76- deficient T cell
    • Yablonski D, Kuhne MR, Kadlecek T, Weiss A. Uncoupling of nonreceptor tyrosine kinases from PLC-γ1 in an SLP-76- deficient T cell. Science 1998 281 : 413 416.
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 89
    • 0021917674 scopus 로고
    • Transmembrane signalling by the T cell antigen receptor. Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores
    • Imboden JB, Stobo JD. Transmembrane signalling by the T cell antigen receptor. Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores. J Exp Med 1985 161 : 446 456.
    • (1985) J Exp Med , vol.161 , pp. 446-456
    • Imboden, J.B.1    Stobo, J.D.2
  • 90
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 1997 15 : 707 747.
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 93
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase Cθ in T cell activation
    • Isakov N, Altman A. Protein kinase Cθ in T cell activation. Annu Rev Immunol 2002 20 : 761 794.
    • (2002) Annu Rev Immunol , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 94
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: A target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • Valverde AM, Sinnett-Smith J, Lint JV, Rozengurt E. Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain. Proc Natl Acad Sci USA 1994 91 : 8572 8576.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8572-8576
    • Valverde, A.M.1    Sinnett-Smith, J.2    Lint, J.V.3    Rozengurt, E.4
  • 95
    • 0034658333 scopus 로고    scopus 로고
    • RasGRP links T-cell receptor signaling to Ras
    • Ebinu JO, et al. RasGRP links T-cell receptor signaling to Ras. Blood 2000 95 : 3199 3203.
    • (2000) Blood , vol.95 , pp. 3199-3203
    • Ebinu, J.O.1
  • 96
    • 0034303371 scopus 로고    scopus 로고
    • RasGRP is essential for mouse thymocyte differentiation and TCR signaling
    • Dower NA, et al. RasGRP is essential for mouse thymocyte differentiation and TCR signaling. Nat Immunol 2000 1 : 317 321.
    • (2000) Nat Immunol , vol.1 , pp. 317-321
    • Dower, N.A.1
  • 97
    • 34147203741 scopus 로고    scopus 로고
    • Unusual interplay of two types of Ras activators, RasGRP and SOS, establishes sensitive and robust Ras activation in lymphocytes
    • Roose JP, Mollenauer M, Ho M, Kurosaki T, Weiss A. Unusual interplay of two types of Ras activators, RasGRP and SOS, establishes sensitive and robust Ras activation in lymphocytes. Mol Cell Biol 2007 27 : 2732 2745.
    • (2007) Mol Cell Biol , vol.27 , pp. 2732-2745
    • Roose, J.P.1    Mollenauer, M.2    Ho, M.3    Kurosaki, T.4    Weiss, A.5
  • 98
    • 18944383647 scopus 로고    scopus 로고
    • A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells
    • Roose JP, Mollenauer M, Gupta VA, Stone J, Weiss A. A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells. Mol Cell Biol 2005 25 : 4426 4441.
    • (2005) Mol Cell Biol , vol.25 , pp. 4426-4441
    • Roose, J.P.1    Mollenauer, M.2    Gupta, V.A.3    Stone, J.4    Weiss, A.5
  • 99
    • 0034724201 scopus 로고    scopus 로고
    • NF-κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ
    • Coudronniere N, Villalba M, Englund N, Altman A. NF-κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ. Proc Natl Acad Sci USA 2000 97 : 3394 3399.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3394-3399
    • Coudronniere, N.1    Villalba, M.2    Englund, N.3    Altman, A.4
  • 100
    • 18844473151 scopus 로고    scopus 로고
    • PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes
    • Sun Z, et al. PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes. Nature 2000 404 : 402 407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1
  • 101
    • 33644772836 scopus 로고    scopus 로고
    • CARMA1 is required for Akt-mediated NF-κB activation in T cells
    • Narayan P, Holt B, Tosti R, Kane LP. CARMA1 is required for Akt-mediated NF-κB activation in T cells. Mol Cell Biol 2006 26 : 2327 2336.
    • (2006) Mol Cell Biol , vol.26 , pp. 2327-2336
    • Narayan, P.1    Holt, B.2    Tosti, R.3    Kane, L.P.4
  • 102
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation
    • Lee KY, D'Acquisto F, Hayden MS, Shim JH, Ghosh S. PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation. Science 2005 308 : 114 118.
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.H.4    Ghosh, S.5
  • 103
    • 0346993668 scopus 로고    scopus 로고
    • CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-θ, Bcl10, and IκB kinase β to the immunological synapse through CARMA1
    • Wang D, et al. CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-θ, Bcl10, and IκB kinase β to the immunological synapse through CARMA1. Mol Cell Biol 2004 24 : 164 171.
    • (2004) Mol Cell Biol , vol.24 , pp. 164-171
    • Wang, D.1
  • 104
    • 8644283766 scopus 로고    scopus 로고
    • The molecular adapter carma1 controls entry of IκB kinase into the central immune synapse
    • Hara H, et al. The molecular adapter carma1 controls entry of IκB kinase into the central immune synapse. J Exp Med 2004 200 : 1167 1177.
    • (2004) J Exp Med , vol.200 , pp. 1167-1177
    • Hara, H.1
  • 105
    • 0037827638 scopus 로고    scopus 로고
    • Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis
    • Jun JE, et al. Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis. Immunity 2003 18 : 751 762.
    • (2003) Immunity , vol.18 , pp. 751-762
    • Jun, J.E.1
  • 106
    • 0034686420 scopus 로고    scopus 로고
    • Protein kinase D. a selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes
    • Matthews SA, Rozengurt E, Cantrell D. Protein kinase D. A selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes. J Exp Med 2000 191 : 2075 2082.
    • (2000) J Exp Med , vol.191 , pp. 2075-2082
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3
  • 107
    • 17144414861 scopus 로고    scopus 로고
    • Protein kinase D1 phosphorylates HDAC7 and induces its nuclear export after TCR activation
    • Parra M, Kasler H, McKinsey TA, Olson EN, Verdin E. Protein kinase D1 phosphorylates HDAC7 and induces its nuclear export after TCR activation. J Biol Chem 2005 280 : 13762 13770.
    • (2005) J Biol Chem , vol.280 , pp. 13762-13770
    • Parra, M.1    Kasler, H.2    McKinsey, T.A.3    Olson, E.N.4    Verdin, E.5
  • 108
    • 15444375044 scopus 로고    scopus 로고
    • Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor-induced Nur77 expression and apoptosis
    • Dequiedt F, et al. Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor-induced Nur77 expression and apoptosis. J Exp Med 2005 201 : 793 804.
    • (2005) J Exp Med , vol.201 , pp. 793-804
    • Dequiedt, F.1
  • 109
    • 0034461022 scopus 로고    scopus 로고
    • Pleiotropic contributions of phospholipase C-γ1 (PLCγ1) to T- cell antigen receptor-mediated signaling: Reconstitution studies of a PLCγ1-deficient Jurkat T-cell line
    • Irvin BJ, Williams BL, Nilson AE, Maynor HO, Abraham RT. Pleiotropic contributions of phospholipase C-γ1 (PLCγ1) to T- cell antigen receptor-mediated signaling: reconstitution studies of a PLCγ1-deficient Jurkat T-cell line. Mol Cell Biol 2000 20 : 9149 9161.
    • (2000) Mol Cell Biol , vol.20 , pp. 9149-9161
    • Irvin, B.J.1    Williams, B.L.2    Nilson, A.E.3    Maynor, H.O.4    Abraham, R.T.5
  • 112
    • 0035911971 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ regulates Ras activation by a novel mechanism
    • Topham MK, Prescott SM. Diacylglycerol kinase ζ regulates Ras activation by a novel mechanism. J Cell Biol 2001 152 : 1135 1143.
    • (2001) J Cell Biol , vol.152 , pp. 1135-1143
    • Topham, M.K.1    Prescott, S.M.2
  • 113
    • 2542444383 scopus 로고    scopus 로고
    • Diacylglycerol-dependent binding recruits PKCθ and RasGRP1 C1 domains to specific subcellular localizations in living T lymphocytes
    • Carrasco S, Merida I. Diacylglycerol-dependent binding recruits PKCθ and RasGRP1 C1 domains to specific subcellular localizations in living T lymphocytes. Mol Biol Cell 2004 15 : 2932 2942.
    • (2004) Mol Biol Cell , vol.15 , pp. 2932-2942
    • Carrasco, S.1    Merida, I.2
  • 114
    • 0035795411 scopus 로고    scopus 로고
    • Role of diacylglycerol kinase α in the attenuation of receptor signaling
    • Sanjuan MA, Jones DR, Izquierdo M, Merida I. Role of diacylglycerol kinase α in the attenuation of receptor signaling. J Cell Biol 2001 153 : 207 220.
    • (2001) J Cell Biol , vol.153 , pp. 207-220
    • Sanjuan, M.A.1    Jones, D.R.2    Izquierdo, M.3    Merida, I.4
  • 115
    • 0034177510 scopus 로고    scopus 로고
    • Coordinate regulation of T cell activation by CD2 and CD28
    • Green JM, Karpitskiy V, Kimzey SL, Shaw AS. Coordinate regulation of T cell activation by CD2 and CD28. J Immunol 2000 164 : 3591 3595.
    • (2000) J Immunol , vol.164 , pp. 3591-3595
    • Green, J.M.1    Karpitskiy, V.2    Kimzey, S.L.3    Shaw, A.S.4
  • 117
    • 0023390431 scopus 로고
    • Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones
    • Jenkins MK, Pardoll DM, Mizuguchi J, Chused TM, Schwartz RH. Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones. Proc Natl Acad Sci USA 1987 84 : 5409 5413.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5409-5413
    • Jenkins, M.K.1    Pardoll, D.M.2    Mizuguchi, J.3    Chused, T.M.4    Schwartz, R.H.5
  • 118
    • 0023266396 scopus 로고
    • Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: Specific induction of a long-lived state of proliferative nonresponsiveness
    • Quill H, Schwartz RH. Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: specific induction of a long-lived state of proliferative nonresponsiveness. J Immunol 1987 138 : 3704 3712.
    • (1987) J Immunol , vol.138 , pp. 3704-3712
    • Quill, H.1    Schwartz, R.H.2
  • 119
    • 0027451433 scopus 로고
    • B7 but not intercellular adhesion molecule-1 costimulation prevents the induction of human alloantigen-specific tolerance
    • Boussiotis VA, Freeman GJ, Gray G, Gribben J, Nadler LM. B7 but not intercellular adhesion molecule-1 costimulation prevents the induction of human alloantigen-specific tolerance. J Exp Med 1993 178 : 1753 1763.
    • (1993) J Exp Med , vol.178 , pp. 1753-1763
    • Boussiotis, V.A.1    Freeman, G.J.2    Gray, G.3    Gribben, J.4    Nadler, L.M.5
  • 120
    • 0034283927 scopus 로고    scopus 로고
    • T cell effector function and anergy avoidance are quantitatively linked to cell division
    • Wells AD, Walsh MC, Sankaran D, Turka LA. T cell effector function and anergy avoidance are quantitatively linked to cell division. J Immunol 2000 165 : 2432 2443.
    • (2000) J Immunol , vol.165 , pp. 2432-2443
    • Wells, A.D.1    Walsh, M.C.2    Sankaran, D.3    Turka, L.A.4
  • 121
    • 27244459060 scopus 로고    scopus 로고
    • A molecular dissection of lymphocyte unresponsiveness induced by sustained calcium signalling
    • Heissmeyer V, et al. A molecular dissection of lymphocyte unresponsiveness induced by sustained calcium signalling. Novartis Found Symp 2005 267 : 165 174.
    • (2005) Novartis Found Symp , vol.267 , pp. 165-174
    • Heissmeyer, V.1
  • 122
    • 12144290293 scopus 로고    scopus 로고
    • Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
    • Heissmeyer V, et al. Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins. Nat Immunol 2004 5 : 255 265.
    • (2004) Nat Immunol , vol.5 , pp. 255-265
    • Heissmeyer, V.1
  • 124
    • 34249736434 scopus 로고    scopus 로고
    • Molecular mechanisms for adaptive tolerance and other T cell anergy models
    • Choi S, Schwartz RH. Molecular mechanisms for adaptive tolerance and other T cell anergy models. Semin Immunol 2007 19 : 140 152.
    • (2007) Semin Immunol , vol.19 , pp. 140-152
    • Choi, S.1    Schwartz, R.H.2
  • 125
    • 0034823168 scopus 로고    scopus 로고
    • Signaling through CD28 and CTLA-4 controls two distinct forms of T cell anergy
    • Wells AD, Walsh MC, Bluestone JA, Turka LA. Signaling through CD28 and CTLA-4 controls two distinct forms of T cell anergy. J Clin Invest 2001 108 : 895 903.
    • (2001) J Clin Invest , vol.108 , pp. 895-903
    • Wells, A.D.1    Walsh, M.C.2    Bluestone, J.A.3    Turka, L.A.4
  • 130
    • 0025096424 scopus 로고
    • + T cells in Staphylococcus enterotoxin B-primed mice
    • + T cells in Staphylococcus enterotoxin B-primed mice. J Exp Med 1990 172 : 1065 1070.
    • (1990) J Exp Med , vol.172 , pp. 1065-1070
    • Kawabe, Y.1    Ochi, A.2
  • 131
    • 0033753014 scopus 로고    scopus 로고
    • Signal transduction by the high-affinity immunoglobulin e receptor FcεRI: Coupling form to function
    • Nadler MJ, Matthews SA, Turner H, Kinet JP. Signal transduction by the high-affinity immunoglobulin E receptor FcεRI: coupling form to function. Adv Immunol 2000 76 : 325 355.
    • (2000) Adv Immunol , vol.76 , pp. 325-355
    • Nadler, M.J.1    Matthews, S.A.2    Turner, H.3    Kinet, J.P.4
  • 132
    • 0033729622 scopus 로고    scopus 로고
    • Roles of mast cells and basophils in innate and acquired immunity
    • Wedemeyer J, Tsai M, Galli SJ. Roles of mast cells and basophils in innate and acquired immunity. Curr Opin Immunol 2000 12 : 624 631.
    • (2000) Curr Opin Immunol , vol.12 , pp. 624-631
    • Wedemeyer, J.1    Tsai, M.2    Galli, S.J.3
  • 133
    • 0036034417 scopus 로고    scopus 로고
    • Macromolecular protein signaling complexes and mast cell responses: A view of the organization of IgE-dependent mast cell signaling
    • Rivera J, et al. Macromolecular protein signaling complexes and mast cell responses: a view of the organization of IgE-dependent mast cell signaling. Mol Immunol 2002 38 : 1253.
    • (2002) Mol Immunol , vol.38 , pp. 1253
    • Rivera, J.1
  • 134
    • 0030018183 scopus 로고    scopus 로고
    • Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells
    • Zhang J, Berenstein E, Evans R, Siraganian R. Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells. J Exp Med 1996 184 : 71 79.
    • (1996) J Exp Med , vol.184 , pp. 71-79
    • Zhang, J.1    Berenstein, E.2    Evans, R.3    Siraganian, R.4
  • 135
    • 0036195935 scopus 로고    scopus 로고
    • Selective loss of gastrointestinal mast cells and impaired immunity in PI3K-deficient mice
    • Fukao T, et al. Selective loss of gastrointestinal mast cells and impaired immunity in PI3K-deficient mice. Nat Immunol 2002 3 : 295 304.
    • (2002) Nat Immunol , vol.3 , pp. 295-304
    • Fukao, T.1
  • 136
    • 7244232917 scopus 로고    scopus 로고
    • Essential role for the p110δ phosphoinositide 3-kinase in the allergic response
    • Ali K, et al. Essential role for the p110δ phosphoinositide 3-kinase in the allergic response. Nature 2004 431 : 1007 1011.
    • (2004) Nature , vol.431 , pp. 1007-1011
    • Ali, K.1
  • 137
    • 0033624638 scopus 로고    scopus 로고
    • Phospholipase Cγ2 is essential in the functions of B cell and several Fc receptors
    • Wang D, et al. Phospholipase Cγ2 is essential in the functions of B cell and several Fc receptors. Immunity 2000 13 : 25 35.
    • (2000) Immunity , vol.13 , pp. 25-35
    • Wang, D.1
  • 138
    • 0026582749 scopus 로고
    • Tyrosine phosphorylation of phospholipase Cγ1 couples the Fcε receptor mediated signal to mast cells secretion
    • Schneider H, Cohen-Dayag A, Pecht I. Tyrosine phosphorylation of phospholipase Cγ1 couples the Fcε receptor mediated signal to mast cells secretion. Int Immunol 1992 4 : 447 453.
    • (1992) Int Immunol , vol.4 , pp. 447-453
    • Schneider, H.1    Cohen-Dayag, A.2    Pecht, I.3
  • 139
    • 0034161386 scopus 로고    scopus 로고
    • Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ
    • Nechushtan H, Leitges M, Cohen C, Kay G, Razin E. Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ. Blood 2000 95 : 1752 1757.
    • (2000) Blood , vol.95 , pp. 1752-1757
    • Nechushtan, H.1    Leitges, M.2    Cohen, C.3    Kay, G.4    Razin, E.5
  • 140
    • 0036258094 scopus 로고    scopus 로고
    • Protein kinase C-δ is a negative regulator of antigen-induced mast cell degranulation
    • Leitges M, et al. Protein kinase C-δ is a negative regulator of antigen-induced mast cell degranulation. Mol Cell Biol 2002 22 : 3970 3980.
    • (2002) Mol Cell Biol , vol.22 , pp. 3970-3980
    • Leitges, M.1
  • 141
    • 33846435302 scopus 로고    scopus 로고
    • An essential role for RasGRP1 in mast cell function and IgE-mediated allergic response
    • Liu Y, Zhu M, Nishida K, Hirano T, Zhang W. An essential role for RasGRP1 in mast cell function and IgE-mediated allergic response. J Exp Med 2007 204 : 93 103.
    • (2007) J Exp Med , vol.204 , pp. 93-103
    • Liu, Y.1    Zhu, M.2    Nishida, K.3    Hirano, T.4    Zhang, W.5
  • 142
    • 0027496310 scopus 로고
    • Activation of MAP kinases, pp90-Rsk and pp70-S6 kinases in mouse mast cells by signaling through the c-Kit receptor tyrosine kinase or FcεRI: Rapamycin inhibits activation of pp70-S6 kinase and proliferation in mouse mast cells
    • Tsai M, Chen RH, Tam SY, Blenis J, Galli SJ. Activation of MAP kinases, pp90-Rsk and pp70-S6 kinases in mouse mast cells by signaling through the c-Kit receptor tyrosine kinase or FcεRI: rapamycin inhibits activation of pp70-S6 kinase and proliferation in mouse mast cells. Eur J Immunol 1993 23 : 3286 3291.
    • (1993) Eur J Immunol , vol.23 , pp. 3286-3291
    • Tsai, M.1    Chen, R.H.2    Tam, S.Y.3    Blenis, J.4    Galli, S.J.5
  • 143
    • 17844383989 scopus 로고    scopus 로고
    • An essential role for phospholipase D in the activation of protein kinase C and degranulation in mast cells
    • Peng Z, Beaven MA. An essential role for phospholipase D in the activation of protein kinase C and degranulation in mast cells. J Immunol 2005 174 : 5201 5208.
    • (2005) J Immunol , vol.174 , pp. 5201-5208
    • Peng, Z.1    Beaven, M.A.2
  • 144
    • 0024308519 scopus 로고
    • Differentiation of second messenger systems in mast cell activation
    • White JR, Zembryki D. Differentiation of second messenger systems in mast cell activation. Agents Actions 1989 27 : 410 413.
    • (1989) Agents Actions , vol.27 , pp. 410-413
    • White, J.R.1    Zembryki, D.2
  • 145
    • 0025129187 scopus 로고
    • Calcium- and guanine-nucleotide-dependent exocytosis in permeabilized rat mast cells. Modulation by protein kinase C
    • Koopmann WR Jr., Jackson RC. Calcium- and guanine-nucleotide-dependent exocytosis in permeabilized rat mast cells. Modulation by protein kinase C. Biochem J 1990 265 : 365 373.
    • (1990) Biochem J , vol.265 , pp. 365-373
    • Koopmann Jr., W.R.1    Jackson, R.C.2
  • 146
    • 0037114147 scopus 로고    scopus 로고
    • Phospholipase Cγ2 is essential for specific functions of FcεR and FcγR
    • Wen R, Jou S-T, Chen Y, Hoffmeyer A, Wang D. Phospholipase Cγ2 is essential for specific functions of FcεR and FcγR. J Immunol 2002 169 : 6743 6752.
    • (2002) J Immunol , vol.169 , pp. 6743-6752
    • Wen, R.1    Jou, S.-T.2    Chen, Y.3    Hoffmeyer, A.4    Wang, D.5
  • 147
    • 0023549568 scopus 로고
    • Synergistic signals in the mechanism of antigen-induced exocytosis in 2H3 cells: Evidence for an unidentified signal required for histamine release
    • Beaven MA, Guthrie DF, Moore JP, Smith GA, Hesketh TR, Metcalfe JC. Synergistic signals in the mechanism of antigen-induced exocytosis in 2H3 cells: evidence for an unidentified signal required for histamine release. J Cell Biol 1987 105 : 1129 1136.
    • (1987) J Cell Biol , vol.105 , pp. 1129-1136
    • Beaven, M.A.1    Guthrie, D.F.2    Moore, J.P.3    Smith, G.A.4    Hesketh, T.R.5    Metcalfe, J.C.6
  • 148
    • 17944377368 scopus 로고    scopus 로고
    • PKCβ modulates antigen receptor signaling via regulation of Btk membrane localization
    • Kang SW, et al. PKCβ modulates antigen receptor signaling via regulation of Btk membrane localization. EMBO J 2001 20 : 5692 5702.
    • (2001) EMBO J , vol.20 , pp. 5692-5702
    • Kang, S.W.1
  • 149
    • 3342912122 scopus 로고    scopus 로고
    • Negative feedback loop in T-cell activation through MAPK-catalyzed threonine phosphorylation of LAT
    • Matsuda S, et al. Negative feedback loop in T-cell activation through MAPK-catalyzed threonine phosphorylation of LAT. EMBO J 2004 23 : 2577 2585.
    • (2004) EMBO J , vol.23 , pp. 2577-2585
    • Matsuda, S.1
  • 150
    • 0036032815 scopus 로고    scopus 로고
    • Signalling role for ARF and phospholipase D in mast cell exocytosis stimulated by crosslinking of the high affinity FcεR1 receptor
    • Cockcroft S, Way G, O'Luanaigh N, Pardo R, Sarri E, Fensome A. Signalling role for ARF and phospholipase D in mast cell exocytosis stimulated by crosslinking of the high affinity FcεR1 receptor. Mol Immunol 2002 38 : 1277 1282.
    • (2002) Mol Immunol , vol.38 , pp. 1277-1282
    • Cockcroft, S.1    Way, G.2    O'Luanaigh, N.3    Pardo, R.4    Sarri, E.5    Fensome, A.6
  • 151
    • 0034948713 scopus 로고    scopus 로고
    • Regulation of mast cell survival by IgE
    • Asai K, et al. Regulation of mast cell survival by IgE. Immunity 2001 14 : 791 800.
    • (2001) Immunity , vol.14 , pp. 791-800
    • Asai, K.1
  • 152
    • 0034948480 scopus 로고    scopus 로고
    • Monomeric IgE stimulates signaling pathways in mast cells that lead to cytokine production and cell survival
    • Kalesnikoff J, et al. Monomeric IgE stimulates signaling pathways in mast cells that lead to cytokine production and cell survival. Immunity 2001 14 : 801 811.
    • (2001) Immunity , vol.14 , pp. 801-811
    • Kalesnikoff, J.1
  • 153
    • 0035803554 scopus 로고    scopus 로고
    • Essential role of the prosurvival Bcl-2 homologue A1 in mast cell survival after allergic activation
    • Xiang Z, Ahmed AA, Moller C, Nakayama K-i, Hatakeyama S, Nilsson G. Essential role of the prosurvival Bcl-2 homologue A1 in mast cell survival after allergic activation. J Exp Med 2001 194 : 1561 1570.
    • (2001) J Exp Med , vol.194 , pp. 1561-1570
    • Xiang, Z.1    Ahmed, A.A.2    Moller, C.3    Nakayama, K.-I.4    Hatakeyama, S.5    Nilsson, G.6
  • 154
    • 0032485483 scopus 로고    scopus 로고
    • Role for interleukin-3 in mast-cell and basophil development and in immunity to parasites
    • Lantz CS, et al. Role for interleukin-3 in mast-cell and basophil development and in immunity to parasites. Nature 1998 392 : 90 93.
    • (1998) Nature , vol.392 , pp. 90-93
    • Lantz, C.S.1
  • 156
    • 0033519629 scopus 로고    scopus 로고
    • Regulation and function of protein kinase B and MAP kinase activation by the IL-5/GM-CSF/IL-3 receptor
    • Dijkers PF, et al. Regulation and function of protein kinase B and MAP kinase activation by the IL-5/GM-CSF/IL-3 receptor. Oncogene 1999 18 : 3334 3342.
    • (1999) Oncogene , vol.18 , pp. 3334-3342
    • Dijkers, P.F.1
  • 157
    • 26044470703 scopus 로고    scopus 로고
    • Biology and epidemiology of Toxoplasma gondii in man and animals
    • Hill DE, Chirukandoth S, Dubey JP. Biology and epidemiology of Toxoplasma gondii in man and animals. Anim Health Res Rev 2005 6 : 41 61.
    • (2005) Anim Health Res Rev , vol.6 , pp. 41-61
    • Hill, D.E.1    Chirukandoth, S.2    Dubey, J.P.3
  • 158
    • 0026021838 scopus 로고
    • + T lymphocytes in IFN-γ production and protective immunity induced by an attenuated Toxoplasma gondii vaccine
    • + T lymphocytes in IFN-γ production and protective immunity induced by an attenuated Toxoplasma gondii vaccine. J Immunol 1991 146 : 286 292.
    • (1991) J Immunol , vol.146 , pp. 286-292
    • Gazzinelli, R.T.1    Hakim, F.T.2    Hieny, S.3    Shearer, G.M.4    Sher, A.5
  • 159
    • 0024438401 scopus 로고
    • Importance of endogenous IFN-γ for prevention of toxoplasmic encephalitis in mice
    • Suzuki Y, Conley FK, Remington JS. Importance of endogenous IFN-γ for prevention of toxoplasmic encephalitis in mice. J Immunol 1989 143 : 2045 2050.
    • (1989) J Immunol , vol.143 , pp. 2045-2050
    • Suzuki, Y.1    Conley, F.K.2    Remington, J.S.3
  • 160
    • 0042854698 scopus 로고    scopus 로고
    • TLR2 as an essential molecule for protective immunity against Toxoplasma gondii infection
    • Mun HS, et al. TLR2 as an essential molecule for protective immunity against Toxoplasma gondii infection. Int Immunol 2003 15 : 1081 1087.
    • (2003) Int Immunol , vol.15 , pp. 1081-1087
    • Mun, H.S.1
  • 161
    • 0037097795 scopus 로고    scopus 로고
    • Cutting edge: MyD88 is required for resistance to Toxoplasma gondii infection and regulates parasite-induced IL-12 production by dendritic cells
    • Scanga CA, et al. Cutting edge: MyD88 is required for resistance to Toxoplasma gondii infection and regulates parasite-induced IL-12 production by dendritic cells. J Immunol 2002 168 : 5997 6001.
    • (2002) J Immunol , vol.168 , pp. 5997-6001
    • Scanga, C.A.1
  • 162
    • 20644433342 scopus 로고    scopus 로고
    • TLR11 activation of dendritic cells by a protozoan profilin-like protein
    • Yarovinsky F, et al. TLR11 activation of dendritic cells by a protozoan profilin-like protein. Science 2005 308 : 1626 1629.
    • (2005) Science , vol.308 , pp. 1626-1629
    • Yarovinsky, F.1
  • 163
    • 33847183077 scopus 로고    scopus 로고
    • Cooperation of Toll-like receptor signals in innate immune defence
    • Trinchieri G, Sher A. Cooperation of Toll-like receptor signals in innate immune defence. Nat Rev Immunol 2007 7 : 179 190.
    • (2007) Nat Rev Immunol , vol.7 , pp. 179-190
    • Trinchieri, G.1    Sher, A.2
  • 164
    • 0034662258 scopus 로고    scopus 로고
    • Cutting edge: IL-12 is required for the maintenance of IFN-γ production in T cells mediating chronic resistance to the intracellular pathogen, Toxoplasma gondii
    • Yap G, Pesin M, Sher A. Cutting edge: IL-12 is required for the maintenance of IFN-γ production in T cells mediating chronic resistance to the intracellular pathogen, Toxoplasma gondii. J Immunol 2000 165 : 628 631.
    • (2000) J Immunol , vol.165 , pp. 628-631
    • Yap, G.1    Pesin, M.2    Sher, A.3
  • 165
    • 0242580118 scopus 로고    scopus 로고
    • Cutting edge: Different toll-like receptor agonists instruct dendritic cells to induce distinct Th responses via differential modulation of extracellular signal-regulated kinase-mitogen-activated protein kinase and c-Fos
    • Agrawal S, et al. Cutting edge: different toll-like receptor agonists instruct dendritic cells to induce distinct Th responses via differential modulation of extracellular signal-regulated kinase-mitogen-activated protein kinase and c-Fos. J Immunol 2003 171 : 4984 4989.
    • (2003) J Immunol , vol.171 , pp. 4984-4989
    • Agrawal, S.1
  • 166
    • 4644244927 scopus 로고    scopus 로고
    • TRAF6-dependent mitogen-activated protein kinase activation differentially regulates the production of interleukin-12 by macrophages in response to Toxoplasma gondii
    • Mason NJ, Fiore J, Kobayashi T, Masek KS, Choi Y, Hunter CA. TRAF6-dependent mitogen-activated protein kinase activation differentially regulates the production of interleukin-12 by macrophages in response to Toxoplasma gondii. Infect Immun 2004 72 : 5662 5667.
    • (2004) Infect Immun , vol.72 , pp. 5662-5667
    • Mason, N.J.1    Fiore, J.2    Kobayashi, T.3    Masek, K.S.4    Choi, Y.5    Hunter, C.A.6
  • 167
    • 0036707521 scopus 로고    scopus 로고
    • PI3K-mediated negative feedback regulation of IL-12 production in DCs
    • Fukao T, et al. PI3K-mediated negative feedback regulation of IL-12 production in DCs. Nat Immunol 2002 3 : 875 881.
    • (2002) Nat Immunol , vol.3 , pp. 875-881
    • Fukao, T.1
  • 168
    • 0037199972 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells
    • Guha M, Mackman N. The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells. J Biol Chem 2002 277 : 32124 32132.
    • (2002) J Biol Chem , vol.277 , pp. 32124-32132
    • Guha, M.1    MacKman, N.2
  • 169
    • 23944486750 scopus 로고    scopus 로고
    • Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3
    • Martin M, Rehani K, Jope RS, Michalek SM. Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3. Nat Immunol 2005 6 : 777 784.
    • (2005) Nat Immunol , vol.6 , pp. 777-784
    • Martin, M.1    Rehani, K.2    Jope, R.S.3    Michalek, S.M.4
  • 170
    • 0141994860 scopus 로고    scopus 로고
    • Protein kinase Cα phosphorylates and negatively regulates diacylglycerol kinase ζ
    • Luo B, Prescott SM, Topham MK. Protein kinase Cα phosphorylates and negatively regulates diacylglycerol kinase ζ. J Biol Chem 2003 278 : 39542 39547.
    • (2003) J Biol Chem , vol.278 , pp. 39542-39547
    • Luo, B.1    Prescott, S.M.2    Topham, M.K.3
  • 171
    • 34250665428 scopus 로고    scopus 로고
    • Proteomics identification of sorting nexin 27 as a diacylglycerol kinase ζ-associated protein: New diacylglycerol kinase roles in endocytic recycling
    • Rincon E, et al. Proteomics identification of sorting nexin 27 as a diacylglycerol kinase ζ-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics 2007 6 : 1073 1087.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1073-1087
    • Rincon, E.1
  • 172
  • 173
    • 0035937193 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ in hypothalamus interacts with long form leptin receptor. Relation to dietary fat and body weight regulation
    • Liu Z, Chang GQ, Leibowitz SF. Diacylglycerol kinase ζ in hypothalamus interacts with long form leptin receptor. Relation to dietary fat and body weight regulation. J Biol Chem 2001 276 : 5900 5907.
    • (2001) J Biol Chem , vol.276 , pp. 5900-5907
    • Liu, Z.1    Chang, G.Q.2    Leibowitz, S.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.