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Volumn 287, Issue 20, 2012, Pages 16656-16669

Novel role for proteinase-activated receptor 2 (PAR2) in membrane trafficking of proteinase-activated receptor 4 (PAR4)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SIGNALS; CELL SURFACES; CLASS A; CO-EXPRESSION; ENDOPLASMIC RETICULUM; G-PROTEIN COUPLED RECEPTORS; HETERODIMERIZATION; INTRACELLULAR TRAFFICKING; MEMBRANE TRAFFICKING; PROTEIN INTERACTION; PROTEIN SEQUENCES; PROTEIN SUBUNITS; PROTEINASE-ACTIVATED RECEPTOR; RECEPTOR ACTIVATION; RECEPTOR LOCALIZATION; RECEPTOR TRAFFICKING; SERINE PROTEASE;

EID: 84860857401     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.315911     Document Type: Article
Times cited : (37)

References (63)
  • 1
    • 60849134552 scopus 로고    scopus 로고
    • Proteinase-activated receptor (PAR) involvement in mediating arthritis pain and inflammation
    • Russell, F. A., and McDougall, J. J. (2009) Proteinase-activated receptor (PAR) involvement in mediating arthritis pain and inflammation. Inflamm. Res. 58, 119-126
    • (2009) Inflamm. Res. , vol.58 , pp. 119-126
    • Russell, F.A.1    McDougall, J.J.2
  • 2
    • 34248377840 scopus 로고    scopus 로고
    • The therapeutic potential of proteinase-activated receptors in arthritis
    • DOI 10.1016/j.coph.2007.01.002, PII S1471489207000471, Respiratory/Musculoskeletal
    • McIntosh, K. A., Plevin, R., Ferrell, W. R., and Lockhart, J. C. (2007) The therapeutic potential of proteinase-activated receptors in arthritis. Curr. Opin. Pharmacol. 7, 334-338 (Pubitemid 46731190)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.3 , pp. 334-338
    • McIntosh, K.A.1    Plevin, R.2    Ferrell, W.R.3    Lockhart, J.C.4
  • 4
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T. K., Hung, D. T., Wheaton, V. I., and Coughlin, S. R. (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64, 1057-1068 (Pubitemid 121001193)
    • (1991) Cell , vol.64 , Issue.6 , pp. 1057-1068
    • Vu, T.-K.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 5
    • 0026072517 scopus 로고
    • Domains specifying thrombin-receptor interaction
    • Vu, T. K., Wheaton, V. I., Hung, D. T., Charo, I., and Coughlin, S. R. (1991) Domains specifying thrombin-receptor interaction. Nature 353, 674-677 (Pubitemid 21912589)
    • (1991) Nature , vol.353 , Issue.6345 , pp. 674-677
    • Vu, T.-K.H.1    Wheaton, V.I.2    Hung, D.T.3    Charot, I.4    Coughlin, S.R.5
  • 6
    • 0028797819 scopus 로고
    • Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system
    • Bouton, M. C., Jandrot-Perrus, M., Moog, S., Cazenave, J. P., Guillin, M. C., and Lanza, F. (1995) Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system. Biochem. J. 305, 635-641
    • (1995) Biochem. J. , vol.305 , pp. 635-641
    • Bouton, M.C.1    Jandrot-Perrus, M.2    Moog, S.3    Cazenave, J.P.4    Guillin, M.C.5    Lanza, F.6
  • 7
    • 0029026320 scopus 로고
    • Determinants of thrombin receptor cleavage. Receptor domains involved, specificity, and role of the P3 aspartate
    • Ishii, K., Gerszten, R., Zheng, Y. W., Welsh, J. B., Turck, C. W., and Coughlin, S. R. (1995) Determinants of thrombin receptor cleavage. Receptor domains involved, specificity, and role of the P3 aspartate. J. Biol. Chem. 270, 16435-16440
    • (1995) J. Biol. Chem. , vol.270 , pp. 16435-16440
    • Ishii, K.1    Gerszten, R.2    Zheng, Y.W.3    Welsh, J.B.4    Turck, C.W.5    Coughlin, S.R.6
  • 9
    • 0030478939 scopus 로고    scopus 로고
    • Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization
    • Shapiro, M. J., Trejo, J., Zeng, D., and Coughlin, S. R. (1996) Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization. J. Biol. Chem. 271, 32874-32880
    • (1996) J. Biol. Chem. , vol.271 , pp. 32874-32880
    • Shapiro, M.J.1    Trejo, J.2    Zeng, D.3    Coughlin, S.R.4
  • 11
    • 0037059795 scopus 로고    scopus 로고
    • β-arrestins regulate protease-activated receptor-1 desensitization but not internalization or down-regulation
    • DOI 10.1074/jbc.M109160200
    • Paing, M. M., Stutts, A. B., Kohout, T. A., Lefkowitz, R. J., and Trejo, J. (2002) β-Arrestins regulate protease-activated receptor-1 desensitization but not internalization or Down-regulation. J. Biol. Chem. 277, 1292-1300 (Pubitemid 34968882)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1292-1300
    • Paing, M.M.1    Stutts, A.B.2    Kohout, T.A.3    Lefkowitz, R.J.4    Trejo, J.5
  • 12
    • 33644864081 scopus 로고    scopus 로고
    • Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization
    • Paing, M. M., Johnston, C. A., Siderovski, D. P., and Trejo, J. (2006) Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization. Mol. Cell. Biol. 26, 3231-3242
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3231-3242
    • Paing, M.M.1    Johnston, C.A.2    Siderovski, D.P.3    Trejo, J.4
  • 13
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • DOI 10.1111/j.1600-0854.2007.00551.x
    • Wolfe, B. L., and Trejo, J. (2007) Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Traffic 8, 462-470 (Pubitemid 46638559)
    • (2007) Traffic , vol.8 , Issue.5 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 14
    • 79959593682 scopus 로고    scopus 로고
    • Structural basis of thrombin-protease-activated receptor interactions
    • Gandhi, P. S., Chen, Z., Appelbaum, E., Zapata, F., and Di Cera, E. (2011) Structural basis of thrombin-protease-activated receptor interactions. IUBMB Life 63, 375-382
    • (2011) IUBMB Life , vol.63 , pp. 375-382
    • Gandhi, P.S.1    Chen, Z.2    Appelbaum, E.3    Zapata, F.4    Di Cera, E.5
  • 15
    • 0029786481 scopus 로고    scopus 로고
    • Mechanisms of desensitization and resensitization of proteinase-activated receptor-2
    • DOI 10.1074/jbc.271.36.22003
    • Böhm, S. K., Khitin, L. M., Grady, E. F., Aponte, G., Payan, D. G., and Bunnett, N. W. (1996) Mechanisms of desensitization and resensitization of proteinase-activated receptor-2. J. Biol. Chem. 271, 22003-22016 (Pubitemid 26303826)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.36 , pp. 22003-22016
    • Bohm, S.K.1    Khitin, L.M.2    Grady, E.F.3    Aponte, G.4    Payan, D.G.5    Bunnett, N.W.6
  • 17
    • 11244328357 scopus 로고    scopus 로고
    • Multiple independent functions of arrestins in the regulation of protease-activated receptor-2 signaling and trafficking
    • DOI 10.1124/mol.104.006072
    • Stalheim, L., Ding, Y., Gullapalli, A., Paing, M. M., Wolfe, B. L., Morris, D. R., and Trejo, J. (2005) Multiple independent functions of arrestins in the regulation of protease-activated receptor-2 signaling and trafficking. Mol. Pharmacol. 67, 78-87 (Pubitemid 40069968)
    • (2005) Molecular Pharmacology , vol.67 , Issue.1 , pp. 78-87
    • Stalheim, L.1    Ding, Y.2    Gullapalli, A.3    Paing, M.M.4    Wolfe, B.L.5    Morris, D.R.6    Trejo, J.7
  • 18
    • 35648992037 scopus 로고    scopus 로고
    • p24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking
    • DOI 10.1074/jbc.M703205200
    • Luo, W., Wang, Y., and Reiser, G. (2007) p24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking. J. Biol. Chem. 282, 30246-30255 (Pubitemid 350035298)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.41 , pp. 30246-30255
    • Luo, W.1    Wang, Y.2    Reiser, G.3
  • 19
    • 79952541443 scopus 로고    scopus 로고
    • Proteinase-activated receptors, nucleotide P2Y receptors, and μ-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking
    • Luo, W., Wang, Y., and Reiser, G. (2011) Proteinase-activated receptors, nucleotide P2Y receptors, and μ-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking. J. Neurochem. 117, 71-81
    • (2011) J. Neurochem. , vol.117 , pp. 71-81
    • Luo, W.1    Wang, Y.2    Reiser, G.3
  • 22
    • 0034682810 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 are shut off with distinct kinetics after activation by thrombin
    • Shapiro, M. J., Weiss, E. J., Faruqi, T. R., and Coughlin, S. R. (2000) Protease-activated receptors 1 and 4 are shut off with distinct kinetics after activation by thrombin. J. Biol. Chem. 275, 25216-25221
    • (2000) J. Biol. Chem. , vol.275 , pp. 25216-25221
    • Shapiro, M.J.1    Weiss, E.J.2    Faruqi, T.R.3    Coughlin, S.R.4
  • 23
    • 0037900130 scopus 로고    scopus 로고
    • Mechanisms of protease-activated receptor-4 actions in cardiomyocytes: Role of Src tyrosine kinase
    • DOI 10.1074/jbc.M213091200
    • Sabri, A., Guo, J., Elouardighi, H., Darrow, A. L., Andrade-Gordon, P., and Steinberg, S. F. (2003) Mechanisms of protease-activated receptor-4 actions in cardiomyocytes. Role of Src tyrosine kinase. J. Biol. Chem. 278, 11714-11720 (Pubitemid 36792735)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11714-11720
    • Sabri, A.1    Guo, J.2    Elouardighi, H.3    Darrow, A.L.4    Andrade-Gordon, P.5    Steinberg, S.F.6
  • 24
  • 25
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Arginine-based endoplasmic reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen, K., Yuan, H., and Schwappach, B. (2005) Hide and run. Arginine-based endoplasmic reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep. 6, 717-722
    • (2005) EMBO Rep. , vol.6 , pp. 717-722
    • Michelsen, K.1    Yuan, H.2    Schwappach, B.3
  • 26
    • 0034189373 scopus 로고    scopus 로고
    • Traffic COPs of the early secretory pathway
    • Barlowe, C. (2000) Traffic COPs of the early secretory pathway. Traffic 1, 371-377
    • (2000) Traffic , vol.1 , pp. 371-377
    • Barlowe, C.1
  • 27
    • 0027459023 scopus 로고
    • Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum
    • Barlowe, C., d'Enfert, C., and Schekman, R. (1993) Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum. J. Biol. Chem. 268, 873-879 (Pubitemid 23019716)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 873-879
    • Barlowe, C.1    D'Enfert, C.2    Schekman, R.3
  • 28
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by sec proteins that drive vesicle budding from the endoplasmic reticulum
    • DOI 10.1016/0092-8674(94)90138-4
    • Barlowe, C., Orci, L., Yeung, T., Hosobuchi, M., Hamamoto, S., Salama, N., Rexach, M. F., Ravazzola, M., Amherdt, M., and Schekman, R. (1994) COPII, a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907 (Pubitemid 24187687)
    • (1994) Cell , vol.77 , Issue.6 , pp. 895-907
    • Barlowe, C.1    Orci, L.2    Yeung, T.3    Hosobuchi, M.4    Hamamoto, S.5    Salama, N.6    Rexach, M.F.7    Ravazzola, M.8    Amherdt, M.9    Schekman, R.10
  • 29
    • 0028971172 scopus 로고
    • Sequential coupling between CopII and CopI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor, M., Bannykh, S. I., Rowe, T., and Balch, W. E. (1995) Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131, 875-893 (Pubitemid 3001804)
    • (1995) Journal of Cell Biology , vol.131 , Issue.4 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 30
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue, N., Schwappach, B., Jan, Y. N., and Jan, L. Y. (1999) A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22, 537-548 (Pubitemid 29159852)
    • (1999) Neuron , vol.22 , Issue.3 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Yuh, N.J.3    Lily, Y.J.4
  • 31
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic, M., Jan, Y. N., and Jan, L. (2000) A trafficking checkpoint controls GABA(B) receptor heterodimerization. Neuron 27, 97-106
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.3
  • 32
    • 0042844727 scopus 로고    scopus 로고
    • Multiple trafficking signals regulate kainate receptor KA2 subunit surface expression
    • Ren, Z., Riley, N. J., Garcia, E. P., Sanders, J. M., Swanson, G. T., and Marshall, J. (2003) Multiple trafficking signals regulate kainate receptor KA2 subunit surface expression. J. Neurosci. 23, 6608-6616 (Pubitemid 36909887)
    • (2003) Journal of Neuroscience , vol.23 , Issue.16 , pp. 6608-6616
    • Ren, Z.1    Riley, N.J.2    Garcia, E.P.3    Sanders, J.M.4    Swanson, G.T.5    Marshall, J.6
  • 33
    • 33744949447 scopus 로고    scopus 로고
    • Intracellular trafficking of KA2 kainate receptors mediated by interactions with coatomer protein complex I (COPI) and 14-3-3 chaperone systems
    • DOI 10.1074/jbc.M512098200
    • Vivithanaporn, P., Yan, S., and Swanson, G. T. (2006) Intracellular trafficking of KA2 kainate receptors mediated by interactions with coatomer protein complex I (COPI) and 14-3-3 chaperone systems. J. Biol. Chem. 281, 15475-15484 (Pubitemid 43855140)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15475-15484
    • Vivithanaporn, P.1    Yan, S.2    Swanson, G.T.3
  • 34
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 Dimers probe the assembly status of multimeric membrane proteins
    • DOI 10.1016/S0960-9822(03)00208-2
    • Yuan, H., Michelsen, K., and Schwappach, B. (2003) 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638-646 (Pubitemid 36453311)
    • (2003) Current Biology , vol.13 , Issue.8 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 35
    • 24344487961 scopus 로고    scopus 로고
    • The regulatory mechanisms of export trafficking of G protein-coupled receptors
    • DOI 10.1016/j.cellsig.2005.05.020, PII S0898656805001269
    • Duvernay, M. T., Filipeanu, C. M., and Wu, G. (2005) The regulatory mechanisms of export trafficking of G protein-coupled receptors. Cell Signal. 17, 1457-1465 (Pubitemid 41253985)
    • (2005) Cellular Signalling , vol.17 , Issue.12 , pp. 1457-1465
    • Duvernay, M.T.1    Filipeanu, C.M.2    Wu, G.3
  • 37
    • 1842791710 scopus 로고    scopus 로고
    • Trypsin IV, a Novel Agonist of Protease-activated Receptors 2 and 4
    • DOI 10.1074/jbc.M312090200
    • Cottrell, G. S., Amadesi, S., Grady, E. F., and Bunnett, N. W. (2004) Trypsin IV, a novel agonist of protease-activated receptors 2 and 4. J. Biol. Chem. 279, 13532-13539 (Pubitemid 38468878)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13532-13539
    • Cottrell, G.S.1    Amadesi, S.2    Grady, E.F.3    Bunnett, N.W.4
  • 38
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • DOI 10.1126/science.1068539
    • Zacharias, D. A., Violin, J. D., Newton, A. C., and Tsien, R. Y. (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916 (Pubitemid 34464897)
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 39
    • 0028358398 scopus 로고
    • Regulation by hypoxia of endothelin-1-stimulated phospholipase D activity in sheep pulmonary artery cultured smooth muscle cells
    • Plevin, R., Kellock, N. A., Wakelam, M. J., and Wadsworth, R. (1994) Regulation by hypoxia of endothelin-1-stimulated phospholipase D activity in sheep pulmonary artery cultured smooth muscle cells. Br. J. Pharmacol. 112, 311-315 (Pubitemid 24151745)
    • (1994) British Journal of Pharmacology , vol.112 , Issue.1 , pp. 311-315
    • Plevin, R.1    Kellock, N.A.2    Wakelam, M.J.O.3    Wadsworth, R.4
  • 40
    • 33745886256 scopus 로고    scopus 로고
    • Syntaxin 16 controls the intracellular sequestration of GLUT4 in 3T3-L1 adipocytes
    • DOI 10.1016/j.bbrc.2006.06.135, PII S0006291X06014094
    • Proctor, K. M., Miller, S. C., Bryant, N. J., and Gould, G. W. (2006) Syntaxin 16 controls the intracellular sequestration of GLUT4 in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 347, 433-438 (Pubitemid 44041435)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.2 , pp. 433-438
    • Proctor, K.M.1    Miller, S.C.M.2    Bryant, N.J.3    Gould, G.W.4
  • 41
    • 23344447877 scopus 로고    scopus 로고
    • The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities
    • DOI 10.1074/jbc.M413475200
    • Wilson, S., Wilkinson, G., and Milligan, G. (2005) The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities. J. Biol. Chem. 280, 28663-28674 (Pubitemid 41105767)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28663-28674
    • Wilson, S.1    Wilkinson, G.2    Milligan, G.3
  • 42
    • 33846030175 scopus 로고    scopus 로고
    • Orexin-1 receptor-cannabinoid CB1 receptor heterodimerization results in both ligand-dependent and -independent coordinated alterations of receptor localization and function
    • DOI 10.1074/jbc.M602494200
    • Ellis, J., Pediani, J. D., Canals, M., Milasta, S., and Milligan, G. (2006) Orexin-1 receptor-cannabinoid CB1 receptor heterodimerization results in both ligand-dependent and -independent coordinated alterations of receptor localization and function. J. Biol. Chem. 281, 38812-38824 (Pubitemid 46042008)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38812-38824
    • Ellis, J.1    Pediani, J.D.2    Canals, M.3    Milasta, S.4    Milligan, G.5
  • 43
    • 33947362780 scopus 로고    scopus 로고
    • 1b-adrenoceptor exists as a higher-order oligomer. Effective oligomerization is required for receptor maturation, surface delivery, and function
    • 1b-adrenoceptor exists as a higher-order oligomer. Effective oligomerization is required for receptor maturation, surface delivery, and function. Mol. Pharmacol. 71, 1015-1029
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1    Canals, M.2    Pediani, J.D.3    Milligan, G.4
  • 44
    • 0035943658 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory κB kinases in NCTC 2544 keratinocytes
    • Kanke, T., Macfarlane, S. R., Seatter, M. J., Davenport, E., Paul, A., McKenzie, R. C., and Plevin, R. (2001) Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory κB kinases in NCTC 2544 keratinocytes. J. Biol. Chem. 276, 31657-31666
    • (2001) J. Biol. Chem. , vol.276 , pp. 31657-31666
    • Kanke, T.1    Macfarlane, S.R.2    Seatter, M.J.3    Davenport, E.4    Paul, A.5    McKenzie, R.C.6    Plevin, R.7
  • 45
    • 0041344648 scopus 로고    scopus 로고
    • Cell surface expression of 5-hydroxytryptamine type 3 receptors is controlled by an endoplasmic reticulum retention signal
    • DOI 10.1074/jbc.M304938200
    • Boyd, G. W., Doward, A. I., Kirkness, E. F., Millar, N. S., and Connolly, C. N. (2003) Cell surface expression of 5-hydroxytryptamine type 3 receptors is controlled by an endoplasmic reticulum retention signal. J. Biol. Chem. 278, 27681-27687 (Pubitemid 36899956)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27681-27687
    • Boyd, G.W.1    Doward, A.I.2    Kirkness, E.F.3    Millar, N.S.4    Connolly, C.N.5
  • 46
    • 0032757001 scopus 로고    scopus 로고
    • N-Linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells
    • Karpa, K. D., Lidow, M. S., Pickering, M. T., Levenson, R., and Bergson, C. (1999) N-Linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells. Mol. Pharmacol. 56, 1071-1078
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1071-1078
    • Karpa, K.D.1    Lidow, M.S.2    Pickering, M.T.3    Levenson, R.4    Bergson, C.5
  • 47
    • 33745937981 scopus 로고    scopus 로고
    • Identification of an endoplasmic reticulum-retention motif in an intracellular loop of the kainate receptor subunit KA2
    • DOI 10.1523/JNEUROSCI.0573-06.2006
    • Nasu-Nishimura, Y., Hurtado, D., Braud, S., Tang, T. T., Isaac, J. T., and Roche, K. W. (2006) Identification of an endoplasmic reticulum-retention motif in an intracellular loop of the kainate receptor subunit KA2. J. Neurosci. 26, 7014-7021 (Pubitemid 44309869)
    • (2006) Journal of Neuroscience , vol.26 , Issue.26 , pp. 7014-7021
    • Nasu-Nishimura, Y.1    Hurtado, D.2    Braud, S.3    Tang, T.T.-T.4    Isaac, J.T.R.5    Roche, K.W.6
  • 49
    • 77956327249 scopus 로고    scopus 로고
    • The roles and mechanisms of PAR4 and P2Y12/phosphatidylinositol 3-kinase pathway in maintaining thrombin-induced platelet aggregation
    • Wu, C. C., Wu, S. Y., Liao, C. Y., Teng, C. M., Wu, Y. C., and Kuo, S. C. (2010) The roles and mechanisms of PAR4 and P2Y12/phosphatidylinositol 3-kinase pathway in maintaining thrombin-induced platelet aggregation. Br. J. Pharmacol. 161, 643-658
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 643-658
    • Wu, C.C.1    Wu, S.Y.2    Liao, C.Y.3    Teng, C.M.4    Wu, Y.C.5    Kuo, S.C.6
  • 50
    • 34249688153 scopus 로고    scopus 로고
    • Proteinase-activated receptor 4 stimulation-induced epithelial- mesenchymal transition in alveolar epithelial cells
    • Ando, S., Otani, H., Yagi, Y., Kawai, K., Araki, H., Fukuhara, S., and Inagaki, C. (2007) Proteinase-activated receptor 4 stimulation-induced epithelial-mesenchymal transition in alveolar epithelial cells. Respir. Res. 8, 31
    • (2007) Respir. Res. , vol.8 , pp. 31
    • Ando, S.1    Otani, H.2    Yagi, Y.3    Kawai, K.4    Araki, H.5    Fukuhara, S.6    Inagaki, C.7
  • 51
  • 53
    • 33745949394 scopus 로고    scopus 로고
    • 14-3-3 proteins: regulation of endoplasmic reticulum localization and surface expression of membrane proteins
    • DOI 10.1016/j.tcb.2006.05.006, PII S0962892406001413
    • Shikano, S., Coblitz, B., Wu, M., and Li, M. (2006) 14-3-3 proteins. Regulation of endoplasmic reticulum localization and surface expression of membrane proteins. Trends Cell Biol. 16, 370-375 (Pubitemid 44062318)
    • (2006) Trends in Cell Biology , vol.16 , Issue.7 , pp. 370-375
    • Shikano, S.1    Coblitz, B.2    Wu, M.3    Li, M.4
  • 54
  • 55
    • 66849132354 scopus 로고    scopus 로고
    • Instability of a class a G protein-coupled receptor oligomer interface
    • Fonseca, J. M., and Lambert, N. A. (2009) Instability of a class a G protein-coupled receptor oligomer interface. Mol. Pharmacol. 75, 1296-1299
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1296-1299
    • Fonseca, J.M.1    Lambert, N.A.2
  • 56
    • 79953192176 scopus 로고    scopus 로고
    • Phosphorylation-dependent C-terminal binding of 14-3-3 proteins promotes cell surface expression of HIV co-receptor GPR15
    • Okamoto, Y., and Shikano, S. (2011) Phosphorylation-dependent C-terminal binding of 14-3-3 proteins promotes cell surface expression of HIV co-receptor GPR15. J. Biol. Chem. 286, 7171-7181
    • (2011) J. Biol. Chem. , vol.286 , pp. 7171-7181
    • Okamoto, Y.1    Shikano, S.2
  • 59
    • 0035816730 scopus 로고    scopus 로고
    • Increased expression of protease-activated receptor-2 (PAR2) and PAR4 in human coronary artery by inflammatory stimuli unveils endothelium-dependent relaxations to PAR2 and PAR4 agonists
    • Hamilton, J. R., Frauman, A. G., and Cocks, T. M. (2001) Increased expression of protease-activated receptor-2 (PAR2) and PAR4 in human coronary artery by inflammatory stimuli unveils endothelium-dependent relaxations to PAR2 and PAR4 agonists. Circ. Res. 89, 92-98 (Pubitemid 34135497)
    • (2001) Circulation Research , vol.89 , Issue.1 , pp. 92-98
    • Hamilton, J.R.1    Frauman, A.G.2    Cocks, T.M.3
  • 60
    • 34247218063 scopus 로고    scopus 로고
    • Cytokine upregulation of proteinase-activated-receptors 2 and 4 expression mediated by p38 MAP kinase and inhibitory kappa B kinase β in human endothelial cells
    • DOI 10.1038/sj.bjp.0707150, PII 0707150
    • Ritchie, E., Saka, M., Mackenzie, C., Drummond, R., Wheeler-Jones, C., Kanke, T., and Plevin, R. (2007) Cytokine up-regulation of proteinase-activated- receptors 2 and 4 expression mediated by p38 MAP kinase and inhibitory κB kinase β in human endothelial cells. Br. J. Pharmacol. 150, 1044-1054 (Pubitemid 46625087)
    • (2007) British Journal of Pharmacology , vol.150 , Issue.8 , pp. 1044-1054
    • Ritchie, E.1    Saka, M.2    MacKenzie, C.3    Drummond, R.4    Wheeler-Jones, C.5    Kanke, T.6    Plevin, R.7
  • 62
    • 61649090828 scopus 로고    scopus 로고
    • Triggering of proteinase-activated receptor 4 leads to joint pain and inflammation in mice
    • McDougall, J. J., Zhang, C., Cellars, L., Joubert, E., Dixon, C. M., and Vergnolle, N. (2009) Triggering of proteinase-activated receptor 4 leads to joint pain and inflammation in mice. Arthritis Rheum. 60, 728-737
    • (2009) Arthritis Rheum. , vol.60 , pp. 728-737
    • McDougall, J.J.1    Zhang, C.2    Cellars, L.3    Joubert, E.4    Dixon, C.M.5    Vergnolle, N.6
  • 63
    • 74049135647 scopus 로고    scopus 로고
    • Proteinase-activated receptor-4 (PAR4) activation leads to sensitization of rat joint primary afferents via a bradykinin B2 receptor-dependent mechanism
    • Russell, F. A., Veldhoen, V. E., Tchitchkan, D., and McDougall, J. J. (2010) Proteinase-activated receptor-4 (PAR4) activation leads to sensitization of rat joint primary afferents via a bradykinin B2 receptor-dependent mechanism. J. Neurophysiol. 103, 155-163
    • (2010) J. Neurophysiol. , vol.103 , pp. 155-163
    • Russell, F.A.1    Veldhoen, V.E.2    Tchitchkan, D.3    McDougall, J.J.4


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