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Volumn 14, Issue 4, 2013, Pages 6649-6673

Diacylglycerol kinases: Regulated controllers of T cell activation, function, and development

Author keywords

Anergy; DGK; Diacylglycerol kinase; iNKT cells; Signal transduction; T cells; Tumor immunity

Indexed keywords

CD28 ANTIGEN; CD69 ANTIGEN; DIACYLGLYCEROL; DIACYLGLYCEROL KINASE; DIACYLGLYCEROL KINASE ALPHA; DIACYLGLYCEROL KINASE BETA; DIACYLGLYCEROL KINASE DELTA; DIACYLGLYCEROL KINASE EPSILON; DIACYLGLYCEROL KINASE ETA; DIACYLGLYCEROL KINASE GAMMA; DIACYLGLYCEROL KINASE IOTA; DIACYLGLYCEROL KINASE KAPPA; DIACYLGLYCEROL KINASE THETA; DIACYLGLYCEROL KINASE ZETA; EARLY GROWTH RESPONSE FACTOR 2; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 2 RECEPTOR ALPHA; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PHOSPHOLIPASE D2; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN KINASE D; S6 KINASE; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 84875472450     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14046649     Document Type: Review
Times cited : (39)

References (122)
  • 1
    • 0035795411 scopus 로고    scopus 로고
    • Role of diacylglycerol kinase α in the attenuation of receptor signaling
    • Sanjuán, M.A.; Jones, D.R.; Izquierdo, M.; Mérida, 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
    • Sanjuán, M.A.1    Jones, D.R.2    Izquierdo, M.3    Mérida, I.4
  • 3
    • 66349133941 scopus 로고    scopus 로고
    • Signaling at the membrane interface by the DGK/SK enzyme family
    • Raben, D.M.; Wattenberg, B.W. Signaling at the membrane interface by the DGK/SK enzyme family. J. Lipid Res. 2008, 50, S35-S39.
    • (2008) J. Lipid Res. , vol.50
    • Raben, D.M.1    Wattenberg, B.W.2
  • 4
    • 0037189475 scopus 로고    scopus 로고
    • Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization
    • Sugiura, M.; Kono, K.; Liu, H.; Shimizugawa, T.; Minekura, H.; Spiegel, S.; Kohama, T. Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization. J. Biol. Chem. 2002, 277, 23294-23300.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23294-23300
    • Sugiura, M.1    Kono, K.2    Liu, H.3    Shimizugawa, T.4    Minekura, H.5    Spiegel, S.6    Kohama, T.7
  • 5
    • 41149157492 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, 410, 631-631.
    • (2008) Biochem. J. , vol.410 , pp. 631
    • Merida, I.1    Avila-Flores, A.2    Merino, E.3
  • 6
    • 0033887478 scopus 로고    scopus 로고
    • Signaling and subcellular targeting by membrane-binding domains
    • Hurley, J.H.; Misra, S. Signaling and subcellular targeting by membrane-binding domains. Annu. Rev. Biophys. Biomol. Struct. 2000, 29, 49-79.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 49-79
    • Hurley, J.H.1    Misra, S.2
  • 7
    • 0034637434 scopus 로고    scopus 로고
    • Subtype-specific translocation of diacylglycerol kinase alpha and gamma 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 alpha and gamma 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
  • 8
    • 0037119466 scopus 로고    scopus 로고
    • Dynamics of diacylglycerol kinase ζ translocation in living T-cells
    • Santos, T.; Carrasco, S.; Jones, D.R.; Mérida, I.; Eguinoa, A. Dynamics of diacylglycerol kinase ζ translocation in living T-cells. 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    Mérida, I.4    Eguinoa, A.5
  • 9
    • 15444373874 scopus 로고    scopus 로고
    • Translocation of diacylglycerol kinase theta 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, W.J. Translocation of diacylglycerol kinase theta 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
  • 10
  • 12
    • 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, J.W.; Walsh, J.P. 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
  • 13
    • 84863332129 scopus 로고    scopus 로고
    • Calcium negatively regulates an intramolecular interaction between the N-terminal recoverin homology and EF-hand motif domains and the C-terminal C1 and catalytic domains of diacylglycerol kinase α
    • Takahashi, M.; Yamamoto, T.; Sakai, H.; Sakane, F. Calcium negatively regulates an intramolecular interaction between the N-terminal recoverin homology and EF-hand motif domains and the C-terminal C1 and catalytic domains of diacylglycerol kinase α. Biochem. Biophys. Res. Commun. 2012, 423, 571-576.
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , pp. 571-576
    • Takahashi, M.1    Yamamoto, T.2    Sakai, H.3    Sakane, F.4
  • 14
    • 36849005359 scopus 로고    scopus 로고
    • Role of the diacylglycerol kinase α-conserved domains in membrane targeting in intact T cells
    • Merino, E.; Sanjuán, M.A.; Moraga, I.; Ciprés, A.; Mérida, 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    Sanjuán, M.A.2    Moraga, I.3    Ciprés, A.4    Mérida, I.5
  • 15
    • 0031033007 scopus 로고    scopus 로고
    • EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes
    • Yamada, K.; Sakane, F.; Matsushima, N.; Kanoh, H. EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes. Biochem. J. 1997, 321, 59-64.
    • (1997) Biochem. J. , vol.321 , pp. 59-64
    • Yamada, K.1    Sakane, F.2    Matsushima, N.3    Kanoh, H.4
  • 16
    • 84871818683 scopus 로고    scopus 로고
    • Induction of filopodia-like protrusions in N1E-115 neuroblastoma cells by diacylglycerol kinase γ independent of its enzymatic activity: Potential novel function of the C-terminal region containing the catalytic domain of diacylglycerol kinase γ
    • Tanino, F.; Maeda, Y.; Sakai, H.; Sakane, F. Induction of filopodia-like protrusions in N1E-115 neuroblastoma cells by diacylglycerol kinase γ independent of its enzymatic activity: Potential novel function of the C-terminal region containing the catalytic domain of diacylglycerol kinase γ. Mol. Cell. Biochem. 2013, 373, 85-93.
    • (2013) Mol. Cell. Biochem. , vol.373 , pp. 85-93
    • Tanino, F.1    Maeda, Y.2    Sakai, H.3    Sakane, F.4
  • 17
    • 28844495301 scopus 로고    scopus 로고
    • Identification and characterization of a novel human type II diacylglycerol kinase, DGKκ
    • Imai, S.; 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.1    Kai, M.2    Yasuda, S.3    Kanoh, H.4    Sakane, F.5
  • 18
    • 0029811987 scopus 로고    scopus 로고
    • Cloning and characterization of a glucocorticoid-induced diacylglycerol kinase
    • Klauck, T.M.; 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
  • 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
    • 42949124488 scopus 로고    scopus 로고
    • Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging
    • Park, W.S.; Heo, W.D.; Whalen, J.H.; O'Rourke, N.A.; Bryan, H.M.; Meyer, T.; Teruel, M.N. Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging. Mol. Cell 2008, 30, 381-392.
    • (2008) Mol. Cell , vol.30 , pp. 381-392
    • Park, W.S.1    Heo, W.D.2    Whalen, J.H.3    O'Rourke, N.A.4    Bryan, H.M.5    Meyer, T.6    Teruel, M.N.7
  • 21
    • 0031565953 scopus 로고    scopus 로고
    • Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130 kDa protein
    • Takeuchi, H.; Kanematsu, T.; Misumi, Y.; Sakane, F.; Konishi, H.; Kikkawa, U.; Watanabe, Y.; Katan, M.; Hirata, M. Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130 kDa protein. Biochim. Biophys. Acta 1997, 1359, 275-285.
    • (1997) Biochim. Biophys. Acta , vol.1359 , pp. 275-285
    • Takeuchi, H.1    Kanematsu, T.2    Misumi, Y.3    Sakane, F.4    Konishi, H.5    Kikkawa, U.6    Watanabe, Y.7    Katan, M.8    Hirata, M.9
  • 22
    • 0037144417 scopus 로고    scopus 로고
    • Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation
    • Imai, S.; Sakane, F.; Kanoh, H. Phorbol ester-regulated oligomerization of diacylglycerol kinase delta 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 delta1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain
    • Imai, S.-I.; Kai, M.; Yamada, K.; Kanoh, H.; Sakane, F. The plasma membrane translocation of diacylglycerol kinase delta1 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.-I.1    Kai, M.2    Yamada, K.3    Kanoh, H.4    Sakane, F.5
  • 25
    • 0031007843 scopus 로고    scopus 로고
    • Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in rat retina
    • Kohyama-Koganeya, A.; Watanabe, M.; Hotta, Y. Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in rat retina. FEBS Lett. 1997, 409, 258-264.
    • (1997) FEBS Lett. , vol.409 , pp. 258-264
    • Kohyama-Koganeya, A.1    Watanabe, M.2    Hotta, Y.3
  • 27
    • 0019829515 scopus 로고
    • The fatty acid composition of phosphatidylinositol from thrombin-stimulated human platelets
    • Prescott, S.M.; Majerus, P.W. The fatty acid composition of phosphatidylinositol from thrombin-stimulated human platelets. J. Biol. Chem. 1981, 256, 579-582.
    • (1981) J. Biol. Chem. , vol.256 , pp. 579-582
    • Prescott, S.M.1    Majerus, P.W.2
  • 28
    • 80054080494 scopus 로고    scopus 로고
    • Regulation and functions of diacylglycerol kinases
    • Shulga, Y.V.; Topham, M.K.; Epand, R.M. Regulation and functions of diacylglycerol kinases. Chem. Rev. 2011, 111, 6186-6208.
    • (2011) Chem. Rev. , vol.111 , pp. 6186-6208
    • Shulga, Y.V.1    Topham, M.K.2    Epand, R.M.3
  • 31
    • 0345687302 scopus 로고    scopus 로고
    • Diacylglycerol kinase-ζ localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins
    • Abramovici, H.; Hogan, A.B.; Obagi, C.; Topham, M.K.; Gee, S.H. 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
  • 32
    • 34250320543 scopus 로고    scopus 로고
    • Morphological changes and spatial regulation of diacylglycerol kinase-ζ, syntrophins, and Rac1 during myoblast fusion
    • Abramovici, H.; Gee, S.H. 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
  • 33
    • 0035937193 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ in hypothalamus interacts with long form leptin receptor
    • Liu, Z.; Chang, G.-Q.; Leibowitz, S.F. Diacylglycerol kinase ζ in hypothalamus interacts with long form leptin receptor. 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
  • 34
    • 67349239306 scopus 로고    scopus 로고
    • Synaptic removal of diacylglycerol by DGKzeta and PSD-95 regulates dendritic spine maintenance
    • Kim, K.; Yang, J.; Zhong, X.-P.; Kim, M.-H.; Kim, Y.S.; Lee, H.W.; Han, S.; Choi, J.; Han, K.; Seo, J.; et al. Synaptic removal of diacylglycerol by DGKzeta and PSD-95 regulates dendritic spine maintenance. EMBO J. 2009, 28, 1170-1179.
    • (2009) EMBO J. , vol.28 , pp. 1170-1179
    • Kim, K.1    Yang, J.2    Zhong, X.-P.3    Kim, M.-H.4    Kim, Y.S.5    Lee, H.W.6    Han, S.7    Choi, J.8    Han, K.9    Seo, J.10
  • 36
    • 0030889241 scopus 로고    scopus 로고
    • Cloning of a novel human diacylglycerol kinase (DGKtheta) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain
    • Houssa, B.; Schaap, D.; van der Wal, J.; Goto, K.; Kondo, H.; Yamakawa, A.; Shibata, M.; Takenawa, T.; Van Blitterswijk, W.J. Cloning of a novel human diacylglycerol kinase (DGKtheta) 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    Schaap, D.2    van der Wal, J.3    Goto, K.4    Kondo, H.5    Yamakawa, A.6    Shibata, M.7    Takenawa, T.8    van Blitterswijk, W.J.9
  • 38
    • 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, S.M.; Topham, M.K. 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
  • 43
    • 84871885298 scopus 로고    scopus 로고
    • Transcriptional regulator early growth response gene 2 (Egr2) is required for T cell anergy in vitro and in vivo
    • Zheng, Y.; Zha, Y.; Driessens, G.; Locke, F.; Gajewski, T.F. Transcriptional regulator early growth response gene 2 (Egr2) is required for T cell anergy in vitro and in vivo. J. Exp. Med. 2012, 209, 2157-2163.
    • (2012) J. Exp. Med. , vol.209 , pp. 2157-2163
    • Zheng, Y.1    Zha, Y.2    Driessens, G.3    Locke, F.4    Gajewski, T.F.5
  • 46
    • 0037443550 scopus 로고    scopus 로고
    • T cell activation in vivo targets diacylglycerol kinase α to the membrane: A novel mechanism for Ras attenuation
    • Sanjuan, M.A.; Pradet-Balade, B.; Jones, D.R.; Martinez-A, C.; Stone, J.C.; Garcia-Sanz, J.A.; Merida, I. 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    Pradet-Balade, B.2    Jones, D.R.3    Martinez-A, C.4    Stone, J.C.5    Garcia-Sanz, J.A.6    Merida, I.7
  • 47
    • 44449117561 scopus 로고    scopus 로고
    • Lck-dependent tyrosine phosphorylation of diacylglycerol kinase α regulates its membrane association in T cells
    • Merino, E.; Ávila-Flores, A.; Shirai, Y.; Moraga, I.; Saito, N.; Mérida, I. Lck-dependent tyrosine phosphorylation of diacylglycerol kinase α regulates its membrane association in T cells. J. Immunol. 2008, 180, 5805-5815.
    • (2008) J. Immunol. , vol.180 , pp. 5805-5815
    • Merino, E.1    Ávila-Flores, A.2    Shirai, Y.3    Moraga, I.4    Saito, N.5    Mérida, I.6
  • 49
    • 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, R.P.; Samelson, L.E. 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
  • 50
    • 0030002904 scopus 로고    scopus 로고
    • Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production
    • Motto, D.G.; Ross, S.E.; Wu, J.; Hendricks-Taylor, L.R.; Koretzky, G.A. 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
  • 51
    • 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, J.B.; Stobo, J.D. 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
  • 53
    • 79959376445 scopus 로고    scopus 로고
    • A cascade of protein kinase C isozymes promotes cytoskeletal polarization in T cells
    • Quann, E.J.; Liu, X.; Altan-Bonnet, G.; Huse, M. A cascade of protein kinase C isozymes promotes cytoskeletal polarization in T cells. Nat. Immunol. 2011, 12, 647-654.
    • (2011) Nat. Immunol. , vol.12 , pp. 647-654
    • Quann, E.J.1    Liu, X.2    Altan-Bonnet, G.3    Huse, M.4
  • 54
    • 33646560593 scopus 로고    scopus 로고
    • Diacylglycerol and protein kinase D localization during T lymphocyte activation
    • Spitaler, M.; Emslie, E.; Wood, C.D.; Cantrell, D. Diacylglycerol and protein kinase D localization during T lymphocyte activation. Immunity 2006, 24, 535-546.
    • (2006) Immunity , vol.24 , pp. 535-546
    • Spitaler, M.1    Emslie, E.2    Wood, C.D.3    Cantrell, D.4
  • 56
    • 0034724201 scopus 로고    scopus 로고
    • NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta
    • Coudronniere, N.; Villalba, M.; Englund, N.; Altman, A. NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta. 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
  • 58
    • 33644772836 scopus 로고    scopus 로고
    • CARMA1 is required for Akt-mediated NF-kappaB activation in T cells
    • Narayan, P.; Holt, B.; Tosti, R.; Kane, L.P. CARMA1 is required for Akt-mediated NF-kappaB 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
  • 59
    • 0346993668 scopus 로고    scopus 로고
    • CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1
    • Wang, D.; Matsumoto, R.; You, Y.; Che, T.; Lin, X.-Y.; Gaffen, S.L.; Lin, X. CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta 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    Matsumoto, R.2    You, Y.3    Che, T.4    Lin, X.-Y.5    Gaffen, S.L.6    Lin, X.7
  • 60
    • 8644283766 scopus 로고    scopus 로고
    • The molecular adapter Carma1 controls entry of IkappaB kinase into the central immune synapse
    • Hara, H.; Bakal, C.; Wada, T.; Bouchard, D.; Rottapel, R.; Saito, T.; Penninger, J.M. The molecular adapter Carma1 controls entry of IkappaB 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    Bakal, C.2    Wada, T.3    Bouchard, D.4    Rottapel, R.5    Saito, T.6    Penninger, J.M.7
  • 61
  • 62
    • 23844509495 scopus 로고    scopus 로고
    • Protein kinase D1 and the beta 1 integrin cytoplasmic domain control beta 1 integrin function via regulation of Rap1 activation
    • Medeiros, R.B.; Dickey, D.M.; Chung, H.; Quale, A.C.; Nagarajan, L.R.; Billadeau, D.D.; Shimizu, Y. Protein kinase D1 and the beta 1 integrin cytoplasmic domain control beta 1 integrin function via regulation of Rap1 activation. Immunity 2005, 23, 213-226.
    • (2005) Immunity , vol.23 , pp. 213-226
    • Medeiros, R.B.1    Dickey, D.M.2    Chung, H.3    Quale, A.C.4    Nagarajan, L.R.5    Billadeau, D.D.6    Shimizu, Y.7
  • 63
    • 34447579251 scopus 로고    scopus 로고
    • The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2
    • Mor, A.; Campi, G.; Du, G.; Zheng, Y.; Foster, D.A.; Dustin, M.L.; Philips, M.R. The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2. Nat. Cell Biol. 2007, 9, 713-719.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 713-719
    • Mor, A.1    Campi, G.2    Du, G.3    Zheng, Y.4    Foster, D.A.5    Dustin, M.L.6    Philips, M.R.7
  • 64
    • 33846438568 scopus 로고    scopus 로고
    • Regulation of mTOR by phosphatidic acid?
    • Foster, D.A. Regulation of mTOR by phosphatidic acid? Cancer Res. 2007, 67, 1-4.
    • (2007) Cancer Res. , vol.67 , pp. 1-4
    • Foster, D.A.1
  • 65
    • 68949103681 scopus 로고    scopus 로고
    • Phosphatidic acid signaling to mTOR: Signals for the survival of human cancer cells
    • Foster, D.A. Phosphatidic acid signaling to mTOR: Signals for the survival of human cancer cells. Biochim. Biophys. Acta 2009, 1791, 949-955.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 949-955
    • Foster, D.A.1
  • 66
    • 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
  • 67
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • Avila-Flores, A. 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
  • 68
    • 49249109489 scopus 로고    scopus 로고
    • Diacylglycerol kinases in immune cell function and self-tolerance
    • Zhong, X.-P.; Guo, R.; Zhou, H.; Liu, C.; Wan, C.-K. Diacylglycerol kinases in immune cell function and self-tolerance. Immunol. Rev. 2008, 224, 249-264.
    • (2008) Immunol. Rev. , vol.224 , pp. 249-264
    • Zhong, X.-P.1    Guo, R.2    Zhou, H.3    Liu, C.4    Wan, C.-K.5
  • 69
    • 0037163130 scopus 로고    scopus 로고
    • Regulation of T cell receptor-induced activation of the Ras-ERK pathway by dacylglycerol kinase ζ
    • Zhong, X.-P.; Hainey, E.A.; Olenchock, B.A.; Zhao, H.; Topham, M.K.; Koretzky, G.A. Regulation of T cell receptor-induced activation of the Ras-ERK pathway by dacylglycerol 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
  • 71
    • 79954618943 scopus 로고    scopus 로고
    • Negative regulation of mTOR activation by diacylglycerol kinases
    • Gorentla, B.K.; Wan, C.-K.; Zhong, X.-P. Negative regulation of mTOR activation by diacylglycerol kinases. Blood 2011, 117, 4022-4031.
    • (2011) Blood , vol.117 , pp. 4022-4031
    • Gorentla, B.K.1    Wan, C.-K.2    Zhong, X.-P.3
  • 72
    • 70349235821 scopus 로고    scopus 로고
    • Molecular origin and functional consequences of digital signaling and hysteresis during Ras activation in lymphocytes
    • Chakraborty, A.K.; Das, J.; Zikherman, J.; Yang, M.; Govern, C.C.; Ho, M.; Weiss, A.; Roose, J. Molecular origin and functional consequences of digital signaling and hysteresis during Ras activation in lymphocytes. Sci. Signal. 2009, 2, pt2.
    • (2009) Sci. Signal. , vol.2
    • Chakraborty, A.K.1    Das, J.2    Zikherman, J.3    Yang, M.4    Govern, C.C.5    Ho, M.6    Weiss, A.7    Roose, J.8
  • 73
    • 18944383647 scopus 로고    scopus 로고
    • A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells
    • Roose, J.P.; Mollenauer, M.; Gupta, V.A.; 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
  • 74
    • 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, J.P.; 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
  • 77
    • 67349243386 scopus 로고    scopus 로고
    • Localized diacylglycerol drives the polarization of the microtubule-organizing center in T cells
    • Quann, E.J.; Merino, E.; Furuta, T.; Huse, M. Localized diacylglycerol drives the polarization of the microtubule-organizing center in T cells. Nat. Immunol. 2009, 10, 627-635.
    • (2009) Nat. Immunol. , vol.10 , pp. 627-635
    • Quann, E.J.1    Merino, E.2    Furuta, T.3    Huse, M.4
  • 78
    • 0035892735 scopus 로고    scopus 로고
    • Differential secretion of Fas ligand-or APO2 ligand/TNF-related apoptosis-inducing ligand-carrying microvesicles during activation-induced death of human T cells
    • Monleón, I.; Martínez-Lorenzo, M.J.; Monteagudo, L.; Lasierra, P.; Taulés, M.; Iturralde, M.; Piñeiro, A.; Larrad, L.; Alava, M.A.; Naval, J.; et al. Differential secretion of Fas ligand-or APO2 ligand/TNF-related apoptosis-inducing ligand-carrying microvesicles during activation-induced death of human T cells. J. Immunol. 2001, 167, 6736-6744.
    • (2001) J. Immunol. , vol.167 , pp. 6736-6744
    • Monleón, I.1    Martínez-Lorenzo, M.J.2    Monteagudo, L.3    Lasierra, P.4    Taulés, M.5    Iturralde, M.6    Piñeiro, A.7    Larrad, L.8    Alava, M.A.9    Naval, J.10
  • 79
    • 33846821720 scopus 로고    scopus 로고
    • Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
    • Zuccato, E.; Blott, E.J.; Holt, O.; Sigismund, S.; Shaw, M.; Bossi, G.; Griffiths, G.M. Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. J. Cell Sci. 2007, 120, 191-199.
    • (2007) J. Cell Sci. , vol.120 , pp. 191-199
    • Zuccato, E.1    Blott, E.J.2    Holt, O.3    Sigismund, S.4    Shaw, M.5    Bossi, G.6    Griffiths, G.M.7
  • 80
    • 79958796052 scopus 로고    scopus 로고
    • Diacylglycerol kinase α regulates the formation and polarisation of mature multivesicular bodies involved in the secretion of Fas ligand-containing exosomes in T lymphocytes
    • Alonso, R.; Mazzeo, C.; Rodriguez, M.C.; Marsh, M.; Fraile-Ramos, A.; Calvo, V.; Avila-Flores, A.; Merida, I.; Izquierdo, M. Diacylglycerol kinase α regulates the formation and polarisation of mature multivesicular bodies involved in the secretion of Fas ligand-containing exosomes in T lymphocytes. Cell Death Differ. 2011, 18, 1161-1173.
    • (2011) Cell Death Differ. , vol.18 , pp. 1161-1173
    • Alonso, R.1    Mazzeo, C.2    Rodriguez, M.C.3    Marsh, M.4    Fraile-Ramos, A.5    Calvo, V.6    Avila-Flores, A.7    Merida, I.8    Izquierdo, M.9
  • 81
    • 0023390431 scopus 로고
    • Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones
    • Jenkins, M.K.; Pardoll, D.M.; Mizuguchi, J.; Chused, T.M.; Schwartz, R.H. 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
  • 82
    • 34249736434 scopus 로고    scopus 로고
    • Molecular mechanisms for adaptive tolerance and other T cell anergy models
    • Choi, S.; Schwartz, R.H. 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
  • 86
    • 62249131518 scopus 로고    scopus 로고
    • Complete but curtailed T-cell response to very low-affinity antigen
    • Zehn, D.; Lee, S.Y.; Bevan, M.J. Complete but curtailed T-cell response to very low-affinity antigen. Nature 2009, 458, 211-214.
    • (2009) Nature , vol.458 , pp. 211-214
    • Zehn, D.1    Lee, S.Y.2    Bevan, M.J.3
  • 90
    • 84857463985 scopus 로고    scopus 로고
    • Differential regulation of primary and memory CD8 T cell immune responses by diacylglycerol kinases
    • Shin, J.; O'Brien, T.F.; Grayson, J.M.; Zhong, X.-P. Differential regulation of primary and memory CD8 T cell immune responses by diacylglycerol kinases. J. Immunol. 2012, 188, 2111-2117.
    • (2012) J. Immunol. , vol.188 , pp. 2111-2117
    • Shin, J.1    O'Brien, T.F.2    Grayson, J.M.3    Zhong, X.-P.4
  • 93
    • 74649085700 scopus 로고    scopus 로고
    • + T cell fate by regulating the expression of transcription factors T-bet and eomesodermin
    • + T cell fate by regulating the expression of transcription factors T-bet and eomesodermin. Immunity 2010, 32, 67-78.
    • (2010) Immunity , vol.32 , pp. 67-78
    • Rao, R.R.1    Li, Q.2    Odunsi, K.3    Shrikant, P.A.4
  • 94
    • 84860237060 scopus 로고    scopus 로고
    • Regulation and function of mTOR signalling in T cell fate decisions
    • Chi, H. Regulation and function of mTOR signalling in T cell fate decisions. Nat. Rev. Immunol. 2012, 12, 325-338.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 325-338
    • Chi, H.1
  • 97
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • Hogg, N.; Patzak, I.; Willenbrock, F. The insider's guide to leukocyte integrin signalling and function. Nat. Rev. Immunol. 2011, 11, 416-426.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 98
    • 27544505630 scopus 로고    scopus 로고
    • The lymphocyte homing receptors: Gatekeepers of the multistep paradigm
    • Sackstein, R. The lymphocyte homing receptors: Gatekeepers of the multistep paradigm. Curr. Opin. Hematol. 2005, 12, 444-450.
    • (2005) Curr. Opin. Hematol. , vol.12 , pp. 444-450
    • Sackstein, R.1
  • 99
    • 84874426205 scopus 로고    scopus 로고
    • Diacylglycerol kinase zeta negatively regulates CXCR4-stimulated T lymphocyte firm arrest to ICAM-1 under shear flow
    • Lee, D.; Kim, J.; Beste, M.T.; Koretzky, G.A.; Hammer, D.A. Diacylglycerol kinase zeta negatively regulates CXCR4-stimulated T lymphocyte firm arrest to ICAM-1 under shear flow. Integr. Biol. 2012, 4, 606-614.
    • (2012) Integr. Biol. , vol.4 , pp. 606-614
    • Lee, D.1    Kim, J.2    Beste, M.T.3    Koretzky, G.A.4    Hammer, D.A.5
  • 100
    • 33746214860 scopus 로고    scopus 로고
    • RasGRP1 transmits prodifferentiation TCR signaling that is crucial for CD4 T cell development
    • Priatel, J.J.; Chen, X.; Dhanji, S.; Abraham, N.; Teh, H.-S. RasGRP1 transmits prodifferentiation TCR signaling that is crucial for CD4 T cell development. J. Immunol. 2006, 177, 1470-1480.
    • (2006) J. Immunol. , vol.177 , pp. 1470-1480
    • Priatel, J.J.1    Chen, X.2    Dhanji, S.3    Abraham, N.4    Teh, H.-S.5
  • 102
    • 0035500758 scopus 로고    scopus 로고
    • Duration and strength of extracellular signal-regulated kinase signals are altered during positive versus negative thymocyte selection
    • Mariathasan, S.; Zakarian, A.; Bouchard, D.; Michie, A.M.; Zúñiga-Pflücker, J.C.; Ohashi, P.S. Duration and strength of extracellular signal-regulated kinase signals are altered during positive versus negative thymocyte selection. J. Immunol. 2001, 167, 4966-4973.
    • (2001) J. Immunol. , vol.167 , pp. 4966-4973
    • Mariathasan, S.1    Zakarian, A.2    Bouchard, D.3    Michie, A.M.4    Zúñiga-Pflücker, J.C.5    Ohashi, P.S.6
  • 103
    • 0034720881 scopus 로고    scopus 로고
    • A motif in the alphabeta T-cell receptor controls positive selection by modulating ERK activity
    • Werlen, G.; Hausmann, B.; Palmer, E. A motif in the alphabeta T-cell receptor controls positive selection by modulating ERK activity. Nature 2000, 406, 422-426.
    • (2000) Nature , vol.406 , pp. 422-426
    • Werlen, G.1    Hausmann, B.2    Palmer, E.3
  • 112
    • 0028863822 scopus 로고
    • Positive selection of mouse NK1+ T cells by CD1-expressing cortical thymocytes
    • Bendelac, A. Positive selection of mouse NK1+ T cells by CD1-expressing cortical thymocytes. J. Exp. Med. 1995, 182, 2091-2096.
    • (1995) J. Exp. Med. , vol.182 , pp. 2091-2096
    • Bendelac, A.1
  • 113
    • 22944442645 scopus 로고    scopus 로고
    • Expansion and long-range differentiation of the NKT cell lineage in mice expressing CD1d exclusively on cortical thymocytes
    • Wei, D.G.; Lee, H.; Park, S.-H.; Beaudoin, L.; Teyton, L.; Lehuen, A.; Bendelac, A. Expansion and long-range differentiation of the NKT cell lineage in mice expressing CD1d exclusively on cortical thymocytes. J. Exp. Med. 2005, 202, 239-248.
    • (2005) J. Exp. Med. , vol.202 , pp. 239-248
    • Wei, D.G.1    Lee, H.2    Park, S.-H.3    Beaudoin, L.4    Teyton, L.5    Lehuen, A.6    Bendelac, A.7
  • 117
    • 0032853934 scopus 로고    scopus 로고
    • Cutting edge: NKT cell development is selectively impaired in Fyn-deficient mice
    • Eberl, G.; Lowin-Kropf, B.; MacDonald, H.R. Cutting edge: NKT cell development is selectively impaired in Fyn-deficient mice. J. Immunol. 1999, 163, 4091-4094.
    • (1999) J. Immunol. , vol.163 , pp. 4091-4094
    • Eberl, G.1    Lowin-Kropf, B.2    McDonald, H.R.3
  • 118
    • 0032723181 scopus 로고    scopus 로고
    • The Src family tyrosine kinase Fyn regulates natural killer T cell development
    • Gadue, P.; Morton, N.; Stein, P.L. The Src family tyrosine kinase Fyn regulates natural killer T cell development. J. Exp. Med. 1999, 190, 1189-1196.
    • (1999) J. Exp. Med. , vol.190 , pp. 1189-1196
    • Gadue, P.1    Morton, N.2    Stein, P.L.3
  • 119
    • 80052689578 scopus 로고    scopus 로고
    • Tight regulation of diacylglycerol-mediated signaling is critical for proper invariant NKT cell development
    • Shen, S.; Wu, J.; Srivatsan, S.; Gorentla, B.K.; Shin, J.; Xu, L.; Zhong, X.-P. Tight regulation of diacylglycerol-mediated signaling is critical for proper invariant NKT cell development. J. Immunol. 2011, 187, 2122-2129.
    • (2011) J. Immunol. , vol.187 , pp. 2122-2129
    • Shen, S.1    Wu, J.2    Srivatsan, S.3    Gorentla, B.K.4    Shin, J.5    Xu, L.6    Zhong, X.-P.7
  • 120
    • 80051775476 scopus 로고    scopus 로고
    • T cells with chimeric antigen receptors have potent antitumor effects and can establish memory in patients with advanced leukemia
    • Kalos, M.; Levine, B.L.; Porter, D.L.; Katz, S.; Grupp, S.A.; Bagg, A.; June, C.H. T cells with chimeric antigen receptors have potent antitumor effects and can establish memory in patients with advanced leukemia. Sci. Trans. Med. 2011, 3, 95ra73.
    • (2011) Sci. Trans. Med. , vol.3
    • Kalos, M.1    Levine, B.L.2    Porter, D.L.3    Katz, S.4    Grupp, S.A.5    Bagg, A.6    June, C.H.7
  • 121
    • 80051720194 scopus 로고    scopus 로고
    • Chimeric antigen receptor-modified T cells in chronic lymphoid leukemia
    • Porter, D.L.; Levine, B.L.; Kalos, M.; Bagg, A.; June, C.H. Chimeric antigen receptor-modified T cells in chronic lymphoid leukemia. N. Engl. J. Med. 2011, 365, 725-733.
    • (2011) N. Engl. J. Med. , vol.365 , pp. 725-733
    • Porter, D.L.1    Levine, B.L.2    Kalos, M.3    Bagg, A.4    June, C.H.5
  • 122
    • 84862838257 scopus 로고    scopus 로고
    • Chimeric antigen receptors for T cell immunotherapy: Current understanding and future directions
    • Curran, K.J.; Pegram, H.J.; Brentjens, R.J. Chimeric antigen receptors for T cell immunotherapy: Current understanding and future directions. J. Gene Med. 2012, 14, 405-415.
    • (2012) J. Gene Med. , vol.14 , pp. 405-415
    • Curran, K.J.1    Pegram, H.J.2    Brentjens, R.J.3


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