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Volumn 112, Issue 2, 2006, Pages 425-439

Mast cell function: Regulation of degranulation by serine/threonine phosphatases

Author keywords

Degranulation; Exocytosis; Mast cells; PP2A; Protein phosphatase; Protein phosphorylation

Indexed keywords

CALCIMYCIN; CALCINEURIN; CALYCULIN A; FOSTRIECIN; MARINE TOXIN; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PHOSPHOSERINE; PHOSPHOTHREONINE; TACROLIMUS;

EID: 33749266374     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2006.04.011     Document Type: Review
Times cited : (28)

References (185)
  • 2
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells
    • Andreassen P.R., Lacroix F.B., Villa-Moruzzi E., and Margolis R.L. Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells. J Cell Biol 141 (1998) 1207-1215
    • (1998) J Cell Biol , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Villa-Moruzzi, E.3    Margolis, R.L.4
  • 3
    • 0026090189 scopus 로고
    • Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C
    • Apgar J.R. Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C. J Cell Biol 112 (1991) 1157-1163
    • (1991) J Cell Biol , vol.112 , pp. 1157-1163
    • Apgar, J.R.1
  • 4
    • 0033651444 scopus 로고    scopus 로고
    • Calcineurin: from structure to function
    • Aramburu J., Rao A., and Klee C.B. Calcineurin: from structure to function. Curr Top Cell Regul 36 (2002) 237-295
    • (2002) Curr Top Cell Regul , vol.36 , pp. 237-295
    • Aramburu, J.1    Rao, A.2    Klee, C.B.3
  • 5
    • 0036118793 scopus 로고    scopus 로고
    • Mast cell-fibroblast interactions: human mast cells as source and inducers of fibroblast and epithelial growth factors
    • Artuc M., Steckelings U.M., and Henz B.M. Mast cell-fibroblast interactions: human mast cells as source and inducers of fibroblast and epithelial growth factors. J Invest Dermatol 118 3 (2002) 391-395
    • (2002) J Invest Dermatol , vol.118 , Issue.3 , pp. 391-395
    • Artuc, M.1    Steckelings, U.M.2    Henz, B.M.3
  • 7
    • 0038579784 scopus 로고    scopus 로고
    • Two modes of exocytosis from synaptosomes are differentially regulated by protein phosphatase types 2A and 2B
    • Baldwin M.L., Rostas J.A., and Sim A.T. Two modes of exocytosis from synaptosomes are differentially regulated by protein phosphatase types 2A and 2B. J Neurochem 85 (2003) 1190-1199
    • (2003) J Neurochem , vol.85 , pp. 1190-1199
    • Baldwin, M.L.1    Rostas, J.A.2    Sim, A.T.3
  • 8
    • 23744445909 scopus 로고    scopus 로고
    • Fibre-type specificity of interleukin-6 gene transcription during muscle contraction in rat: association with calcineurin activity
    • Banzet S., Koulmann N., Simler N., Birot O., Sanchez H., Chapot R., et al. Fibre-type specificity of interleukin-6 gene transcription during muscle contraction in rat: association with calcineurin activity. J Physiol 566 (2005) 839-847
    • (2005) J Physiol , vol.566 , pp. 839-847
    • Banzet, S.1    Koulmann, N.2    Simler, N.3    Birot, O.4    Sanchez, H.5    Chapot, R.6
  • 9
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D. Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci 21 (1996) 407-412
    • (1996) Trends Biochem Sci , vol.21 , pp. 407-412
    • Barford, D.1
  • 10
    • 0035955397 scopus 로고    scopus 로고
    • Regulation of immunoglobulin E-mediated secretion by protein phosphatases in human basophils and mast cells of skin and lung
    • Bastan R., Peirce M.J., and Peachell P.T. Regulation of immunoglobulin E-mediated secretion by protein phosphatases in human basophils and mast cells of skin and lung. Eur J Pharmacol 430 (2001) 135-141
    • (2001) Eur J Pharmacol , vol.430 , pp. 135-141
    • Bastan, R.1    Peirce, M.J.2    Peachell, P.T.3
  • 11
    • 0030457522 scopus 로고    scopus 로고
    • Downstream signals initiated in mast cells by Fc epsilon RI and other receptors
    • Beaven M.A., and Baumgartner R.A. Downstream signals initiated in mast cells by Fc epsilon RI and other receptors. Curr Opin Immunol 8 (1996) 766-772
    • (1996) Curr Opin Immunol , vol.8 , pp. 766-772
    • Beaven, M.A.1    Baumgartner, R.A.2
  • 12
    • 0029856725 scopus 로고    scopus 로고
    • cAMP counter-regulates insulin-mediated protein phosphatase-2A inactivation in rat skeletal muscle cells
    • Begum N., and Ragolia L. cAMP counter-regulates insulin-mediated protein phosphatase-2A inactivation in rat skeletal muscle cells. J Biol Chem 271 (1996) 31166-31171
    • (1996) J Biol Chem , vol.271 , pp. 31166-31171
    • Begum, N.1    Ragolia, L.2
  • 13
    • 33645037097 scopus 로고    scopus 로고
    • The striatin family: a new signaling platform in dendritic spines
    • (Paris)
    • Benoist M., Gaillard S., and Castets F. The striatin family: a new signaling platform in dendritic spines. J Physiol 99 (2006) 146-158 (Paris)
    • (2006) J Physiol , vol.99 , pp. 146-158
    • Benoist, M.1    Gaillard, S.2    Castets, F.3
  • 14
    • 0034867321 scopus 로고    scopus 로고
    • Tryptase and agonists of PAR-2 induce the proliferation of human airway smooth muscle cells
    • Berger P., Perng D.W., Thabrew H., Compton S.J., Cairns J.A., McEuen A.R., et al. Tryptase and agonists of PAR-2 induce the proliferation of human airway smooth muscle cells. J Appl Physiol 91 3 (2001) 1372-1379
    • (2001) J Appl Physiol , vol.91 , Issue.3 , pp. 1372-1379
    • Berger, P.1    Perng, D.W.2    Thabrew, H.3    Compton, S.J.4    Cairns, J.A.5    McEuen, A.R.6
  • 15
    • 10344222887 scopus 로고    scopus 로고
    • The ins and outs of IgE-dependent mast-cell exocytosis
    • Blank U., and Rivera J. The ins and outs of IgE-dependent mast-cell exocytosis. Trends Immunol 25 (2004) 266-273
    • (2004) Trends Immunol , vol.25 , pp. 266-273
    • Blank, U.1    Rivera, J.2
  • 16
    • 0036034297 scopus 로고    scopus 로고
    • SNAREs and associated regulators in the control of exocytosis in the RBL-2H3 mast cell line
    • Blank U., Cyprien B., Martin-Verdeaux S., Paumet F., Pombo I., Rivera J., et al. SNAREs and associated regulators in the control of exocytosis in the RBL-2H3 mast cell line. Mol Immunol 38 (2002) 1341-1345
    • (2002) Mol Immunol , vol.38 , pp. 1341-1345
    • Blank, U.1    Cyprien, B.2    Martin-Verdeaux, S.3    Paumet, F.4    Pombo, I.5    Rivera, J.6
  • 18
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen M. Combinatorial control of protein phosphatase-1. Trends Biochem Sci 26 (2001) 426-431
    • (2001) Trends Biochem Sci , vol.26 , pp. 426-431
    • Bollen, M.1
  • 19
    • 0036498531 scopus 로고    scopus 로고
    • Signaling by protein phosphatases in the nucleus
    • Bollen M., and Beullens M. Signaling by protein phosphatases in the nucleus. Trends Cell Biol 12 (2002) 138-145
    • (2002) Trends Cell Biol , vol.12 , pp. 138-145
    • Bollen, M.1    Beullens, M.2
  • 21
    • 22044432763 scopus 로고    scopus 로고
    • The use of okadaic acid to elucidate the intracellular role(s) of protein phosphatase 2A: lessons from the mast cell model system
    • Boudreau R.T., and Hoskin D.W. The use of okadaic acid to elucidate the intracellular role(s) of protein phosphatase 2A: lessons from the mast cell model system. Int Immunopharmacol 5 (2005) 1507-1518
    • (2005) Int Immunopharmacol , vol.5 , pp. 1507-1518
    • Boudreau, R.T.1    Hoskin, D.W.2
  • 22
    • 0037085442 scopus 로고    scopus 로고
    • Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells
    • Boudreau R.T., Garduno R., and Lin T.J. Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells. J Biol Chem 277 (2002) 5322-5329
    • (2002) J Biol Chem , vol.277 , pp. 5322-5329
    • Boudreau, R.T.1    Garduno, R.2    Lin, T.J.3
  • 23
    • 7644221446 scopus 로고    scopus 로고
    • Phosphatase inhibition potentiates IL-6 production by mast cells in response to FcepsilonRI-mediated activation: involvement of p38 MAPK
    • Boudreau R.T., Hoskin D.W., and Lin T.J. Phosphatase inhibition potentiates IL-6 production by mast cells in response to FcepsilonRI-mediated activation: involvement of p38 MAPK. J Leukoc Biol 76 (2004) 1075-1081
    • (2004) J Leukoc Biol , vol.76 , pp. 1075-1081
    • Boudreau, R.T.1    Hoskin, D.W.2    Lin, T.J.3
  • 24
    • 0037308329 scopus 로고    scopus 로고
    • The role of the mast cell in asthma: a reassessment
    • Bradding P. The role of the mast cell in asthma: a reassessment. Curr Opin Allergy Clin Immunol 3 1 (2003) 45-50
    • (2003) Curr Opin Allergy Clin Immunol , vol.3 , Issue.1 , pp. 45-50
    • Bradding, P.1
  • 25
    • 0035787093 scopus 로고    scopus 로고
    • The role of protein phosphatase-1 in insulin action
    • Brady M.J., and Saltiel A.R. The role of protein phosphatase-1 in insulin action. Recent Prog Horm Res 56 (2001) 157-173
    • (2001) Recent Prog Horm Res , vol.56 , pp. 157-173
    • Brady, M.J.1    Saltiel, A.R.2
  • 26
    • 14744295367 scopus 로고    scopus 로고
    • The re-emergence of the mast cell as a pivotal cell in asthma pathogenesis
    • Brightling C.E., and Bradding P. The re-emergence of the mast cell as a pivotal cell in asthma pathogenesis. Curr Allergy Asthma Rep 5 (2005) 130-135
    • (2005) Curr Allergy Asthma Rep , vol.5 , pp. 130-135
    • Brightling, C.E.1    Bradding, P.2
  • 30
    • 0035625681 scopus 로고    scopus 로고
    • The level of the glycogen targetting regulatory subunit R5 of protein phosphatase 1 is decreased in the livers of insulin-dependent diabetic rats and starved rats
    • Browne G.J., Delibegovic M., Keppens S., Stalmans W., and Cohen P.T. The level of the glycogen targetting regulatory subunit R5 of protein phosphatase 1 is decreased in the livers of insulin-dependent diabetic rats and starved rats. Biochem J 360 (2001) 449-459
    • (2001) Biochem J , vol.360 , pp. 449-459
    • Browne, G.J.1    Delibegovic, M.2    Keppens, S.3    Stalmans, W.4    Cohen, P.T.5
  • 31
    • 0037317592 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2
    • Brush M.H., Weiser D.C., and Shenolikar S. Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol 23 (2003) 1292-1303
    • (2003) Mol Cell Biol , vol.23 , pp. 1292-1303
    • Brush, M.H.1    Weiser, D.C.2    Shenolikar, S.3
  • 32
    • 33646563150 scopus 로고    scopus 로고
    • Childhood asthma in South London: trends in prevalence and use of medical services 1991-2002
    • Butland B.K., Strachan D.P., Crawley-Boevey E.E., and Anderson H.R. Childhood asthma in South London: trends in prevalence and use of medical services 1991-2002. Thorax 61 (2006) 383-387
    • (2006) Thorax , vol.61 , pp. 383-387
    • Butland, B.K.1    Strachan, D.P.2    Crawley-Boevey, E.E.3    Anderson, H.R.4
  • 35
    • 31844438968 scopus 로고    scopus 로고
    • A prospective study of asthma desensitization in 1182 children, 592 asthmatic children and 590 nonatopic controls
    • Cantani A., and Micera M. A prospective study of asthma desensitization in 1182 children, 592 asthmatic children and 590 nonatopic controls. Eur Rev Med Pharmacol Sci 9 (2005) 325-329
    • (2005) Eur Rev Med Pharmacol Sci , vol.9 , pp. 325-329
    • Cantani, A.1    Micera, M.2
  • 36
    • 0036014530 scopus 로고    scopus 로고
    • Distribution and degranulation of airway mast cells in normal and asthmatic subjects
    • Carroll N.G., Mutavdzic S., and James A.L. Distribution and degranulation of airway mast cells in normal and asthmatic subjects. Eur Respir J 19 (2002) 879-885
    • (2002) Eur Respir J , vol.19 , pp. 879-885
    • Carroll, N.G.1    Mutavdzic, S.2    James, A.L.3
  • 37
    • 0036341331 scopus 로고    scopus 로고
    • Increased mast cells and neutrophils in submucosal mucous glands and mucus plugging in patients with asthma
    • Carroll N.G., Mutavdzic S., and James A.L. Increased mast cells and neutrophils in submucosal mucous glands and mucus plugging in patients with asthma. Thorax 57 (2002) 677-682
    • (2002) Thorax , vol.57 , pp. 677-682
    • Carroll, N.G.1    Mutavdzic, S.2    James, A.L.3
  • 38
    • 0036010598 scopus 로고    scopus 로고
    • Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution
    • Ceulemans H., Stalmans W., and Bollen M. Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. Bioessays 24 (2002) 371-381
    • (2002) Bioessays , vol.24 , pp. 371-381
    • Ceulemans, H.1    Stalmans, W.2    Bollen, M.3
  • 39
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • Chen J., Martin B.L., and Brautigan D.L. Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science 257 (1992) 1261-1264
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 41
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
    • Chheda M.G., Ashery U., Thakur P., Rettig J., and Sheng Z.H. Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex. Nat Cell Biol 3 (2001) 331-338
    • (2001) Nat Cell Biol , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 42
    • 0035234311 scopus 로고    scopus 로고
    • Protein phosphatase 5 in signal transduction
    • Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab 12 (2001) 28-32
    • (2001) Trends Endocrinol Metab , vol.12 , pp. 28-32
    • Chinkers, M.1
  • 43
    • 0001093453 scopus 로고
    • Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C
    • Choi O.H., Adelstein R.S., and Beaven M.A. Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C. J Biol Chem 269 (1994) 536-541
    • (1994) J Biol Chem , vol.269 , pp. 536-541
    • Choi, O.H.1    Adelstein, R.S.2    Beaven, M.A.3
  • 44
    • 0023088497 scopus 로고
    • Inhibition of IgE-dependent histamine release from human dispersed lung mast cells by anti-allergic drugs and salbutamol
    • Church M.K., and Hiroi J. Inhibition of IgE-dependent histamine release from human dispersed lung mast cells by anti-allergic drugs and salbutamol. Br J Pharmacol 90 (1987) 421-429
    • (1987) Br J Pharmacol , vol.90 , pp. 421-429
    • Church, M.K.1    Hiroi, J.2
  • 45
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 58 (1989) 453-508
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 46
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1-targeted in many directions
    • Cohen P.T. Protein phosphatase 1-targeted in many directions. J Cell Sci 115 (2002) 241-256
    • (2002) J Cell Sci , vol.115 , pp. 241-256
    • Cohen, P.T.1
  • 47
    • 20444422553 scopus 로고    scopus 로고
    • Protein phosphatase 4-from obscurity to vital functions
    • Cohen P.T., Philp A., and Vazquez-Martin C. Protein phosphatase 4-from obscurity to vital functions. FEBS Lett 579 (2005) 3278-3286
    • (2005) FEBS Lett , vol.579 , pp. 3278-3286
    • Cohen, P.T.1    Philp, A.2    Vazquez-Martin, C.3
  • 49
    • 0030047451 scopus 로고    scopus 로고
    • High complexity in the expression of the B′ subunit of protein phosphatase 2A0. Evidence for the existence of at least seven novel isoforms
    • Csortos C., Zolnierowicz S., Bako E., Durbin S.D., and DePaoli-Roach A.A. High complexity in the expression of the B′ subunit of protein phosphatase 2A0. Evidence for the existence of at least seven novel isoforms. J Biol Chem 271 (1996) 2578-2588
    • (1996) J Biol Chem , vol.271 , pp. 2578-2588
    • Csortos, C.1    Zolnierowicz, S.2    Bako, E.3    Durbin, S.D.4    DePaoli-Roach, A.A.5
  • 52
    • 0037073758 scopus 로고    scopus 로고
    • Mapping the protein phosphatase-2B anchoring site on AKAP79. Binding and inhibition of phosphatase activity are mediated by residues 315-360
    • Dell'Acqua M.L., Dodge K.L., Tavalin S.J., and Scott J.D. Mapping the protein phosphatase-2B anchoring site on AKAP79. Binding and inhibition of phosphatase activity are mediated by residues 315-360. J Biol Chem 277 (2002) 48796-48802
    • (2002) J Biol Chem , vol.277 , pp. 48796-48802
    • Dell'Acqua, M.L.1    Dodge, K.L.2    Tavalin, S.J.3    Scott, J.D.4
  • 53
    • 13844312725 scopus 로고    scopus 로고
    • Dual specificity protein phosphatases: therapeutic targets for cancer and Alzheimer's disease. An overview of the protein tyrosine phosphatase superfamily
    • Ducruet A.P., Vogt A., Wipf P., Lazo J.S., Wang W.Q., Sun J.P., et al. Dual specificity protein phosphatases: therapeutic targets for cancer and Alzheimer's disease. An overview of the protein tyrosine phosphatase superfamily. Annu Rev Pharmacol Toxicol 45 (2005) 725-750
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 725-750
    • Ducruet, A.P.1    Vogt, A.2    Wipf, P.3    Lazo, J.S.4    Wang, W.Q.5    Sun, J.P.6
  • 54
    • 0037422556 scopus 로고    scopus 로고
    • Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins
    • Dulubova I., Yamaguchi T., Arac D., Li H., Huryeva I., Min S.W., et al. Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins. Proc Natl Acad Sci U S A 100 (2003) 32-37
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 32-37
    • Dulubova, I.1    Yamaguchi, T.2    Arac, D.3    Li, H.4    Huryeva, I.5    Min, S.W.6
  • 55
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff M.P., Johnson D.F., Moorhead G., Cohen P.T., Cohen P., and Barford D. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J 16 (1997) 1876-1887
    • (1997) EMBO J , vol.16 , pp. 1876-1887
    • Egloff, M.P.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.4    Cohen, P.5    Barford, D.6
  • 56
    • 0028256156 scopus 로고
    • Effect of okadaic acid on immunologic and non-immunologic histamine release in rat mast cells
    • Estevez M.D., Vieytes M.R., Louzao M.C., and Botana L.M. Effect of okadaic acid on immunologic and non-immunologic histamine release in rat mast cells. Biochem Pharmacol 47 (1994) 591-593
    • (1994) Biochem Pharmacol , vol.47 , pp. 591-593
    • Estevez, M.D.1    Vieytes, M.R.2    Louzao, M.C.3    Botana, L.M.4
  • 57
    • 2942584972 scopus 로고    scopus 로고
    • Dephosphorylation of RNA polymerase I by Fcp1p is required for efficient rRNA synthesis
    • Fath S., Kobor M.S., Philippi A., Greenblatt J., and Tschochner H. Dephosphorylation of RNA polymerase I by Fcp1p is required for efficient rRNA synthesis. J Biol Chem 279 (2004) 25251-25259
    • (2004) J Biol Chem , vol.279 , pp. 25251-25259
    • Fath, S.1    Kobor, M.S.2    Philippi, A.3    Greenblatt, J.4    Tschochner, H.5
  • 58
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • Favre B., Turowski P., and Hemmings B.A. Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. J Biol Chem 272 (1997) 13856-13863
    • (1997) J Biol Chem , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 59
    • 0033199617 scopus 로고    scopus 로고
    • Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: effects on GTP/GDP binding and cellular distribution
    • Fitzgerald M.L., and Reed G.L. Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: effects on GTP/GDP binding and cellular distribution. Biochem J 342 (1999) 353-360
    • (1999) Biochem J , vol.342 , pp. 353-360
    • Fitzgerald, M.L.1    Reed, G.L.2
  • 61
    • 0028813436 scopus 로고
    • The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells
    • Fruman D.A., Bierer B.E., Benes J.E., Burakoff S.J., Austen K.F., and Katz H.R. The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells. J Immunol 154 (1995) 1846-1851
    • (1995) J Immunol , vol.154 , pp. 1846-1851
    • Fruman, D.A.1    Bierer, B.E.2    Benes, J.E.3    Burakoff, S.J.4    Austen, K.F.5    Katz, H.R.6
  • 62
  • 63
    • 0033065245 scopus 로고    scopus 로고
    • SNAREs and SNARE regulators in membrane fusion and exocytosis
    • Gerst J.E. SNAREs and SNARE regulators in membrane fusion and exocytosis. Cell Mol Life Sci 55 (1999) 707-734
    • (1999) Cell Mol Life Sci , vol.55 , pp. 707-734
    • Gerst, J.E.1
  • 64
    • 0027245528 scopus 로고
    • Intraepithelial mast cells in allergic and nonallergic asthma. Assessment using bronchial brushings
    • Gibson P.G., Allen C.J., Yang J.P., Wong B.J., Dolovich J., Denburg J., et al. Intraepithelial mast cells in allergic and nonallergic asthma. Assessment using bronchial brushings. Am Rev Respir Dis 148 (1993) 80-86
    • (1993) Am Rev Respir Dis , vol.148 , pp. 80-86
    • Gibson, P.G.1    Allen, C.J.2    Yang, J.P.3    Wong, B.J.4    Dolovich, J.5    Denburg, J.6
  • 65
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP20
    • Gorina S., and Pavletich N.P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP20. Science 274 (1996) 1001-1005
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 66
    • 0344665680 scopus 로고    scopus 로고
    • Transgenic and knockout models of PP2A
    • Gotz J., and Schild A. Transgenic and knockout models of PP2A. Methods Enzymol 366 (2003) 390-403
    • (2003) Methods Enzymol , vol.366 , pp. 390-403
    • Gotz, J.1    Schild, A.2
  • 67
    • 0032514680 scopus 로고    scopus 로고
    • Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Calpha
    • Gotz J., Probst A., Ehler E., Hemmings B., and Kues W. Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Calpha. Proc Natl Acad Sci U S A 95 (1998) 12370-12375
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12370-12375
    • Gotz, J.1    Probst, A.2    Ehler, E.3    Hemmings, B.4    Kues, W.5
  • 68
    • 85047692201 scopus 로고
    • Activation of protein kinases and the inactivation of protein phosphatase 2A in tumour necrosis factor and interleukin-1 signal-transduction pathways
    • Guy G.R., Philp R., and Tan Y.H. Activation of protein kinases and the inactivation of protein phosphatase 2A in tumour necrosis factor and interleukin-1 signal-transduction pathways. Eur J Biochem 229 (1995) 503-511
    • (1995) Eur J Biochem , vol.229 , pp. 503-511
    • Guy, G.R.1    Philp, R.2    Tan, Y.H.3
  • 69
    • 0028218772 scopus 로고
    • Cell proliferation status, cytokine action and protein tyrosine phosphorylation modulate leukotriene biosynthesis in a basophil leukaemia and a mastocytoma cell line
    • Hagmann W. Cell proliferation status, cytokine action and protein tyrosine phosphorylation modulate leukotriene biosynthesis in a basophil leukaemia and a mastocytoma cell line. Biochem J 299 Pt 2 (1994) 467-472
    • (1994) Biochem J , vol.299 , Issue.PART 2 , pp. 467-472
    • Hagmann, W.1
  • 70
    • 0030475207 scopus 로고    scopus 로고
    • 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Calpha correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer
    • Hansra G., Bornancin F., Whelan R., Hemmings B.A., and Parker P.J. 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Calpha correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer. J Biol Chem 271 (1996) 32785-32788
    • (1996) J Biol Chem , vol.271 , pp. 32785-32788
    • Hansra, G.1    Bornancin, F.2    Whelan, R.3    Hemmings, B.A.4    Parker, P.J.5
  • 71
    • 0025953404 scopus 로고
    • Use of okadaic acid to inhibit protein phosphatases in intact cells
    • Hardie D.G., Haystead T.A., and Sim A.T. Use of okadaic acid to inhibit protein phosphatases in intact cells. Methods Enzymol 201 (1991) 469-476
    • (1991) Methods Enzymol , vol.201 , pp. 469-476
    • Hardie, D.G.1    Haystead, T.A.2    Sim, A.T.3
  • 72
    • 0024991506 scopus 로고
    • Identification of an autoinhibitory domain in calcineurin
    • Hashimoto Y., Perrino B.A., and Soderling T.R. Identification of an autoinhibitory domain in calcineurin. J Biol Chem 265 (1990) 1924-1927
    • (1990) J Biol Chem , vol.265 , pp. 1924-1927
    • Hashimoto, Y.1    Perrino, B.A.2    Soderling, T.R.3
  • 73
    • 0032563347 scopus 로고    scopus 로고
    • Purification of protein phosphatase 4 catalytic subunit: inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters
    • Hastie C.J., and Cohen P.T. Purification of protein phosphatase 4 catalytic subunit: inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters. FEBS Lett 431 (1998) 357-361
    • (1998) FEBS Lett , vol.431 , pp. 357-361
    • Hastie, C.J.1    Cohen, P.T.2
  • 74
    • 0036285634 scopus 로고    scopus 로고
    • Mathematical models of protein kinase signal transduction
    • Heinrich R., Neel B.G., and Rapoport T.A. Mathematical models of protein kinase signal transduction. Mol Cell 9 (2002) 957-970
    • (2002) Mol Cell , vol.9 , pp. 957-970
    • Heinrich, R.1    Neel, B.G.2    Rapoport, T.A.3
  • 75
    • 0025275038 scopus 로고
    • alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure
    • Hemmings B.A., Adams-Pearson C., Maurer F., Muller P., Goris J., Merlevede W., et al. alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure. Biochemistry 29 (1990) 3166-3173
    • (1990) Biochemistry , vol.29 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3    Muller, P.4    Goris, J.5    Merlevede, W.6
  • 76
    • 0027279893 scopus 로고
    • Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing
    • Hendrix P., Mayer-Jackel R.E., Cron P., Goris J., Hofsteenge J., Merlevede W., et al. Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing. J Biol Chem 268 (1993) 15267-15276
    • (1993) J Biol Chem , vol.268 , pp. 15267-15276
    • Hendrix, P.1    Mayer-Jackel, R.E.2    Cron, P.3    Goris, J.4    Hofsteenge, J.5    Merlevede, W.6
  • 77
    • 0036676438 scopus 로고    scopus 로고
    • Nonreceptor protein tyrosine and lipid phosphatases in type I fc(epsilon) receptor-mediated activation of mast cells and basophils
    • Heneberg P., and Draber P. Nonreceptor protein tyrosine and lipid phosphatases in type I fc(epsilon) receptor-mediated activation of mast cells and basophils. Int Arch Allergy Immunol 128 (2002) 253-263
    • (2002) Int Arch Allergy Immunol , vol.128 , pp. 253-263
    • Heneberg, P.1    Draber, P.2
  • 78
    • 0036198540 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells
    • Holst J., Sim A.T., and Ludowyke R.I. Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells. Mol Biol Cell 13 (2002) 1083-1098
    • (2002) Mol Biol Cell , vol.13 , pp. 1083-1098
    • Holst, J.1    Sim, A.T.2    Ludowyke, R.I.3
  • 79
    • 0031915128 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)
    • Huang X., and Honkanen R.E. Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC). J Biol Chem 273 (1998) 1462-1468
    • (1998) J Biol Chem , vol.273 , pp. 1462-1468
    • Huang, X.1    Honkanen, R.E.2
  • 80
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard M.J., and Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem Sci 18 (1993) 172-177
    • (1993) Trends Biochem Sci , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 81
    • 0024427914 scopus 로고
    • Characterization of a high-affinity monoclonal antibody to calcineurin whose epitope defines a new structural domain of calcineurin A
    • Hubbard M.J., and Klee C.B. Characterization of a high-affinity monoclonal antibody to calcineurin whose epitope defines a new structural domain of calcineurin A. Eur J Biochem 185 (1989) 411-418
    • (1989) Eur J Biochem , vol.185 , pp. 411-418
    • Hubbard, M.J.1    Klee, C.B.2
  • 82
    • 0024550177 scopus 로고
    • Functional domain structure of calcineurin A: mapping by limited proteolysis
    • Hubbard M.J., and Klee C.B. Functional domain structure of calcineurin A: mapping by limited proteolysis. Biochemistry 28 (1989) 1868-1874
    • (1989) Biochemistry , vol.28 , pp. 1868-1874
    • Hubbard, M.J.1    Klee, C.B.2
  • 83
    • 0031840312 scopus 로고    scopus 로고
    • Direct evidence that FK506 inhibition of FcepsilonRI-mediated exocytosis from RBL mast cells involves calcineurin
    • Hultsch T., Brand P., Lohmann S., Saloga J., Kincaid R.L., and Knop J. Direct evidence that FK506 inhibition of FcepsilonRI-mediated exocytosis from RBL mast cells involves calcineurin. Arch Dermatol Res 290 (1998) 258-263
    • (1998) Arch Dermatol Res , vol.290 , pp. 258-263
    • Hultsch, T.1    Brand, P.2    Lohmann, S.3    Saloga, J.4    Kincaid, R.L.5    Knop, J.6
  • 84
    • 30344460002 scopus 로고    scopus 로고
    • Gi protein-mediated translocation of serine/threonine phosphatase to the plasma membrane and apoptosis of ovarian cancer cell in response to gonadotropin-releasing hormone antagonist cetrorelix
    • Imai A., Sugiyama M., Furui T., and Tamaya T. Gi protein-mediated translocation of serine/threonine phosphatase to the plasma membrane and apoptosis of ovarian cancer cell in response to gonadotropin-releasing hormone antagonist cetrorelix. J Obstet Gynaecol 26 (2006) 37-41
    • (2006) J Obstet Gynaecol , vol.26 , pp. 37-41
    • Imai, A.1    Sugiyama, M.2    Furui, T.3    Tamaya, T.4
  • 85
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R., and Sudhof T.C. Membrane fusion and exocytosis. Annu Rev Biochem 68 (1999) 863-911
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 86
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V., and Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353 (2001) 417-439
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 89
    • 10344225084 scopus 로고    scopus 로고
    • Neuromedin U elicits cytokine release in murine Th2-type T cell clone D10, G4.1
    • Johnson E.N., Appelbaum E.R., Carpenter D.C., Cox R.F., Disa J., Foley J.J., et al. Neuromedin U elicits cytokine release in murine Th2-type T cell clone D10, G4.1. J Immunol 173 (2004) 7230-7238
    • (2004) J Immunol , vol.173 , pp. 7230-7238
    • Johnson, E.N.1    Appelbaum, E.R.2    Carpenter, D.C.3    Cox, R.F.4    Disa, J.5    Foley, J.J.6
  • 90
    • 0037013237 scopus 로고    scopus 로고
    • Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid
    • Jones J.A., and Hannun Y.A. Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid. J Biol Chem 277 (2002) 15530-15538
    • (2002) J Biol Chem , vol.277 , pp. 15530-15538
    • Jones, J.A.1    Hannun, Y.A.2
  • 91
    • 26444524348 scopus 로고    scopus 로고
    • Identification of a novel phosphatidic acid binding domain in protein phosphatase-1
    • Jones J.A., Rawles R., and Hannun Y.A. Identification of a novel phosphatidic acid binding domain in protein phosphatase-1. Biochemistry 44 (2005) 13235-13245
    • (2005) Biochemistry , vol.44 , pp. 13235-13245
    • Jones, J.A.1    Rawles, R.2    Hannun, Y.A.3
  • 92
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen L.M., Dutil E.M., and Newton A.C. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 5 (1995) 1394-1403
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 93
    • 0026023150 scopus 로고
    • Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes
    • (erratum appears in Biochemistry 1991 May 28;30(21): 5328)
    • Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., and Hemmings B.A. Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes. (erratum appears in Biochemistry 1991 May 28;30(21): 5328). Biochemistry 30 (1991) 89-97
    • (1991) Biochemistry , vol.30 , pp. 89-97
    • Khew-Goodall, Y.1    Mayer, R.E.2    Maurer, F.3    Stone, S.R.4    Hemmings, B.A.5
  • 94
    • 0037162448 scopus 로고    scopus 로고
    • Calpain-dependent cleavage of cain/cabin1 activates calcineurin to mediate calcium-triggered cell death
    • Kim M.J., Jo D.G., Hong G.S., Kim B.J., Lai M., Cho D.H., et al. Calpain-dependent cleavage of cain/cabin1 activates calcineurin to mediate calcium-triggered cell death. Proc Natl Acad Sci U S A 99 (2002) 9870-9875
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9870-9875
    • Kim, M.J.1    Jo, D.G.2    Hong, G.S.3    Kim, B.J.4    Lai, M.5    Cho, D.H.6
  • 95
    • 0029888742 scopus 로고    scopus 로고
    • The effect of okadaic acid on histamine release, cell morphology and phosphorylation in rat basophilic leukemia (RBL-2H3) cells, human basophils and rat peritoneal mast cells
    • Kitani S., Teshima R., Nonomura Y., Morita Y., and Ito K. The effect of okadaic acid on histamine release, cell morphology and phosphorylation in rat basophilic leukemia (RBL-2H3) cells, human basophils and rat peritoneal mast cells. Int Arch Allergy Immunol 110 (1996) 339-347
    • (1996) Int Arch Allergy Immunol , vol.110 , pp. 339-347
    • Kitani, S.1    Teshima, R.2    Nonomura, Y.3    Morita, Y.4    Ito, K.5
  • 96
    • 0034130649 scopus 로고    scopus 로고
    • Priming in exocytosis: attaining fusion-competence after vesicle docking
    • Klenchin V.A., and Martin T.F. Priming in exocytosis: attaining fusion-competence after vesicle docking. Biochimie 82 (2000) 399-407
    • (2000) Biochimie , vol.82 , pp. 399-407
    • Klenchin, V.A.1    Martin, T.F.2
  • 97
    • 0034177877 scopus 로고    scopus 로고
    • An essential role of mast cells in the development of airway hyperresponsiveness in a murine asthma model
    • Kobayashi T., Miura T., Haba T., Sato M., Serizawa I., Nagai H., et al. An essential role of mast cells in the development of airway hyperresponsiveness in a murine asthma model. J Immunol 164 (2000) 3855-3861
    • (2000) J Immunol , vol.164 , pp. 3855-3861
    • Kobayashi, T.1    Miura, T.2    Haba, T.3    Sato, M.4    Serizawa, I.5    Nagai, H.6
  • 98
    • 0035013541 scopus 로고    scopus 로고
    • Inhibition of mast cell tryptase by inhaled APC 366 attenuates allergen-induced late-phase airway obstruction in asthma
    • Krishna M.T., Chauhan A., Little L., Sampson K., Hawksworth R., Mant T., et al. Inhibition of mast cell tryptase by inhaled APC 366 attenuates allergen-induced late-phase airway obstruction in asthma. J Allergy Clin Immunol 107 (2001) 1039-1045
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 1039-1045
    • Krishna, M.T.1    Chauhan, A.2    Little, L.3    Sampson, K.4    Hawksworth, R.5    Mant, T.6
  • 100
    • 0036729230 scopus 로고    scopus 로고
    • Modeling allergic asthma in mice: pitfalls and opportunities
    • Kumar R.K., and Foster P.S. Modeling allergic asthma in mice: pitfalls and opportunities. Am J Respir Cell Mol Biol 27 (2002) 267-272
    • (2002) Am J Respir Cell Mol Biol , vol.27 , pp. 267-272
    • Kumar, R.K.1    Foster, P.S.2
  • 101
    • 0026685033 scopus 로고
    • Distinct cellular expression of calcineurin A alpha and A beta in rat brain
    • Kuno T., Mukai H., Ito A., Chang C.D., Kishima K., Saito N., et al. Distinct cellular expression of calcineurin A alpha and A beta in rat brain. J Neurochem 58 (1992) 1643-1651
    • (1992) J Neurochem , vol.58 , pp. 1643-1651
    • Kuno, T.1    Mukai, H.2    Ito, A.3    Chang, C.D.4    Kishima, K.5    Saito, N.6
  • 102
    • 0034602315 scopus 로고    scopus 로고
    • The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis
    • Lai M.M., Luo H.R., Burnett P.E., Hong J.J., and Snyder S.H. The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis. J Biol Chem 275 (2000) 34017-34020
    • (2000) J Biol Chem , vol.275 , pp. 34017-34020
    • Lai, M.M.1    Luo, H.R.2    Burnett, P.E.3    Hong, J.J.4    Snyder, S.H.5
  • 103
    • 0034130493 scopus 로고    scopus 로고
    • Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells
    • Lang T., Wacker I., Wunderlich I., Rohrbach A., Giese G., Soldati T., et al. Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells. Biophys J 78 (2000) 2863-2877
    • (2000) Biophys J , vol.78 , pp. 2863-2877
    • Lang, T.1    Wacker, I.2    Wunderlich, I.3    Rohrbach, A.4    Giese, G.5    Soldati, T.6
  • 104
    • 24344487343 scopus 로고    scopus 로고
    • A-kinase-anchoring proteins
    • Langeberg L.K., and Scott J.D. A-kinase-anchoring proteins. J Cell Sci 118 (2005) 3217-3220
    • (2005) J Cell Sci , vol.118 , pp. 3217-3220
    • Langeberg, L.K.1    Scott, J.D.2
  • 105
    • 0027184102 scopus 로고
    • Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase
    • Lee J., and Stock J. Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase. J Biol Chem 268 (1993) 19192-19195
    • (1993) J Biol Chem , vol.268 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 106
    • 33644524383 scopus 로고    scopus 로고
    • B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK
    • Letourneux C., Rocher G., and Porteu F. B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK. EMBO J 25 (2006) 727-738
    • (2006) EMBO J , vol.25 , pp. 727-738
    • Letourneux, C.1    Rocher, G.2    Porteu, F.3
  • 107
    • 0036161826 scopus 로고    scopus 로고
    • Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A
    • Li X., and Virshup D.M. Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A. Eur J Biochem 269 (2002) 546-552
    • (2002) Eur J Biochem , vol.269 , pp. 546-552
    • Li, X.1    Virshup, D.M.2
  • 108
    • 33744721514 scopus 로고    scopus 로고
    • Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle
    • Li M., Stefansson B., Wang W., Schaefer E.M., and Brautigan D.L. Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle. Cell Signal (2005)
    • (2005) Cell Signal
    • Li, M.1    Stefansson, B.2    Wang, W.3    Schaefer, E.M.4    Brautigan, D.L.5
  • 109
    • 10344237581 scopus 로고    scopus 로고
    • Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha
    • Lu Q., Pallas D.C., Surks H.K., Baur W.E., Mendelsohn M.E., and Karas R.H. Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha. Proc Natl Acad Sci U S A 101 (2004) 17126-17131
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17126-17131
    • Lu, Q.1    Pallas, D.C.2    Surks, H.K.3    Baur, W.E.4    Mendelsohn, M.E.5    Karas, R.H.6
  • 110
    • 0028340905 scopus 로고
    • Calcium-independent secretion by ATP gamma S from a permeabilized rat basophilic leukaemia cell line (RBL-2H3)
    • Ludowyke R.I., and Scurr L.L. Calcium-independent secretion by ATP gamma S from a permeabilized rat basophilic leukaemia cell line (RBL-2H3). Cell Signal 6 (1994) 223-231
    • (1994) Cell Signal , vol.6 , pp. 223-231
    • Ludowyke, R.I.1    Scurr, L.L.2
  • 111
    • 0024362253 scopus 로고
    • Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells
    • Ludowyke R.I., Peleg I., Beaven M.A., and Adelstein R.S. Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. J Biol Chem 264 (1989) 12492-12501
    • (1989) J Biol Chem , vol.264 , pp. 12492-12501
    • Ludowyke, R.I.1    Peleg, I.2    Beaven, M.A.3    Adelstein, R.S.4
  • 112
    • 0030456713 scopus 로고    scopus 로고
    • Calcium ionophore-induced secretion from mast cells correlates with myosin light chain phosphorylation by protein kinase C
    • Ludowyke R.I., Scurr L.L., and McNally C.M. Calcium ionophore-induced secretion from mast cells correlates with myosin light chain phosphorylation by protein kinase C. J Immunol 157 (1996) 5130-5138
    • (1996) J Immunol , vol.157 , pp. 5130-5138
    • Ludowyke, R.I.1    Scurr, L.L.2    McNally, C.M.3
  • 113
    • 0032296566 scopus 로고    scopus 로고
    • Inhibition of antigen and calcium ionophore induced secretion from RBL-2H3 cells by phosphatase inhibitors
    • Ludowyke R.I., Warton K., and Scurr L.L. Inhibition of antigen and calcium ionophore induced secretion from RBL-2H3 cells by phosphatase inhibitors. Cell Biol Int 22 (1998) 855-865
    • (1998) Cell Biol Int , vol.22 , pp. 855-865
    • Ludowyke, R.I.1    Warton, K.2    Scurr, L.L.3
  • 114
    • 0034008926 scopus 로고    scopus 로고
    • Transient translocation and activation of protein phosphatase 2A during mast cell secretion
    • Ludowyke R.I., Holst J., Mudge L.M., and Sim A.T. Transient translocation and activation of protein phosphatase 2A during mast cell secretion. J Biol Chem 275 (2000) 6144-6152
    • (2000) J Biol Chem , vol.275 , pp. 6144-6152
    • Ludowyke, R.I.1    Holst, J.2    Mudge, L.M.3    Sim, A.T.4
  • 115
    • 0029822999 scopus 로고    scopus 로고
    • Potential allergens stimulate the release of mediators of the allergic response from cells of mast cell lineage in the absence of sensitization with antigen-specific IgE
    • Machado D.C., Horton D., Harrop R., Peachell P.T., and Helm B.A. Potential allergens stimulate the release of mediators of the allergic response from cells of mast cell lineage in the absence of sensitization with antigen-specific IgE. Eur J Immunol 26 (1996) 2972-2980
    • (1996) Eur J Immunol , vol.26 , pp. 2972-2980
    • Machado, D.C.1    Horton, D.2    Harrop, R.3    Peachell, P.T.4    Helm, B.A.5
  • 116
    • 0034866533 scopus 로고    scopus 로고
    • cAmp modulates exocytotic kinetics and increases quantal size in chromaffin cells
    • Machado J.D., Morales A., Gomez J.F., and Borges R. cAmp modulates exocytotic kinetics and increases quantal size in chromaffin cells. Mol Pharmacol 60 (2001) 514-520
    • (2001) Mol Pharmacol , vol.60 , pp. 514-520
    • Machado, J.D.1    Morales, A.2    Gomez, J.F.3    Borges, R.4
  • 117
    • 0035853727 scopus 로고    scopus 로고
    • Phosphorylation of the N-ethylmaleimide-sensitive factor is associated with depolarization-dependent neurotransmitter release from synaptosomes
    • Matveeva E.A., Whiteheart S.W., Vanaman T.C., and Slevin J.T. Phosphorylation of the N-ethylmaleimide-sensitive factor is associated with depolarization-dependent neurotransmitter release from synaptosomes. J Biol Chem 276 (2001) 12174-12181
    • (2001) J Biol Chem , vol.276 , pp. 12174-12181
    • Matveeva, E.A.1    Whiteheart, S.W.2    Vanaman, T.C.3    Slevin, J.T.4
  • 119
    • 0033613083 scopus 로고    scopus 로고
    • Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation
    • McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., et al. Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation. Biochemistry 38 (1999) 12943-12949
    • (1999) Biochemistry , vol.38 , pp. 12943-12949
    • McAvoy, T.1    Allen, P.B.2    Obaishi, H.3    Nakanishi, H.4    Takai, Y.5    Greengard, P.6
  • 120
    • 0030586955 scopus 로고    scopus 로고
    • Assignment of human protein phosphatase 2A regulatory subunit genes b56alpha, b56beta, b56gamma, b56delta, and b56epsilon (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 → p12
    • McCright B., Brothman A.R., and Virshup D.M. Assignment of human protein phosphatase 2A regulatory subunit genes b56alpha, b56beta, b56gamma, b56delta, and b56epsilon (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 → p12. Genomics 36 (1996) 168-170
    • (1996) Genomics , vol.36 , pp. 168-170
    • McCright, B.1    Brothman, A.R.2    Virshup, D.M.3
  • 121
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright B., Rivers A.M., Audlin S., and Virshup D.M. The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J Biol Chem 271 (1996) 22081-22089
    • (1996) J Biol Chem , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 122
    • 30744432348 scopus 로고    scopus 로고
    • Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins
    • Meiselbach H., Sticht H., and Enz R. Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins. Chem Biol 13 (2006) 49-59
    • (2006) Chem Biol , vol.13 , pp. 49-59
    • Meiselbach, H.1    Sticht, H.2    Enz, R.3
  • 123
    • 0034050449 scopus 로고    scopus 로고
    • WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A
    • Moreno C.S., Park S., Nelson K., Ashby D., Hubalek F., Lane W.S., et al. WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. J Biol Chem 275 (2000) 5257-5263
    • (2000) J Biol Chem , vol.275 , pp. 5257-5263
    • Moreno, C.S.1    Park, S.2    Nelson, K.3    Ashby, D.4    Hubalek, F.5    Lane, W.S.6
  • 124
    • 0026200344 scopus 로고
    • Protein phosphatases and DNA tumor viruses: transformation through the back door?
    • Mumby M.C., and Walter G. Protein phosphatases and DNA tumor viruses: transformation through the back door?. Cell Regul 2 (1991) 589-598
    • (1991) Cell Regul , vol.2 , pp. 589-598
    • Mumby, M.C.1    Walter, G.2
  • 126
    • 0037009005 scopus 로고    scopus 로고
    • Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex
    • Nunbhakdi-Craig V., Machleidt T., Ogris E., Bellotto D., White III C.L., and Sontag E. Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex. J Cell Biol 158 (2002) 967-978
    • (2002) J Cell Biol , vol.158 , pp. 967-978
    • Nunbhakdi-Craig, V.1    Machleidt, T.2    Ogris, E.3    Bellotto, D.4    White III, C.L.5    Sontag, E.6
  • 127
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., et al. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem 274 (1999) 14382-14391
    • (1999) J Biol Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6
  • 128
    • 0030821233 scopus 로고    scopus 로고
    • Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen
    • Ogris E., Gibson D.M., and Pallas D.C. Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen. Oncogene 15 (1997) 911-917
    • (1997) Oncogene , vol.15 , pp. 911-917
    • Ogris, E.1    Gibson, D.M.2    Pallas, D.C.3
  • 129
    • 25144448762 scopus 로고    scopus 로고
    • Mast cell mediators in airway remodeling
    • Oh C.K. Mast cell mediators in airway remodeling. Chem Immunol Allergy 87 (2005) 85-100
    • (2005) Chem Immunol Allergy , vol.87 , pp. 85-100
    • Oh, C.K.1
  • 131
    • 0037421222 scopus 로고    scopus 로고
    • Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy
    • Oliveria S.F., Gomez L.L., and Dell'Acqua M.L. Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy. J Cell Biol 160 (2003) 101-112
    • (2003) J Cell Biol , vol.160 , pp. 101-112
    • Oliveria, S.F.1    Gomez, L.L.2    Dell'Acqua, M.L.3
  • 132
    • 25144514081 scopus 로고    scopus 로고
    • Mast cells in allergic airway disease and chronic rhinosinusitis
    • Pawankar R. Mast cells in allergic airway disease and chronic rhinosinusitis. Chem Immunol Allergy 87 (2005) 111-129
    • (2005) Chem Immunol Allergy , vol.87 , pp. 111-129
    • Pawankar, R.1
  • 133
    • 18744396140 scopus 로고    scopus 로고
    • Targeting the mast cell in asthma
    • Peachell P. Targeting the mast cell in asthma. Curr Opin Pharmacol 5 (2005) 251-256
    • (2005) Curr Opin Pharmacol , vol.5 , pp. 251-256
    • Peachell, P.1
  • 134
    • 0027205530 scopus 로고
    • Regulation of human lung mast cell function by phosphatase inhibitors
    • Peachell P.T., and Munday M.R. Regulation of human lung mast cell function by phosphatase inhibitors. J Immunol 151 (1993) 3808-3816
    • (1993) J Immunol , vol.151 , pp. 3808-3816
    • Peachell, P.T.1    Munday, M.R.2
  • 135
    • 0029818995 scopus 로고    scopus 로고
    • Regulation of human basophil function by phosphatase inhibitors
    • Peirce M.J., Warner J.A., Munday M.R., and Peachell P.T. Regulation of human basophil function by phosphatase inhibitors. Br J Pharmacol 119 (1996) 446-453
    • (1996) Br J Pharmacol , vol.119 , pp. 446-453
    • Peirce, M.J.1    Warner, J.A.2    Munday, M.R.3    Peachell, P.T.4
  • 136
    • 0031023947 scopus 로고    scopus 로고
    • Preliminary characterization of the role of protein serine/threonine phosphatases in the regulation of human lung mast cell function
    • Peirce M.J., Cox S.E., Munday M.R., and Peachell P.T. Preliminary characterization of the role of protein serine/threonine phosphatases in the regulation of human lung mast cell function. Br J Pharmacol 120 (1997) 239-246
    • (1997) Br J Pharmacol , vol.120 , pp. 239-246
    • Peirce, M.J.1    Cox, S.E.2    Munday, M.R.3    Peachell, P.T.4
  • 137
    • 0034986439 scopus 로고    scopus 로고
    • Ca(2+)- and myristoylation-dependent association of calcineurin with phosphatidylserine
    • Perrino B.A., and Martin B.A. Ca(2+)- and myristoylation-dependent association of calcineurin with phosphatidylserine. J Biochem 129 (2001) 835-841
    • (2001) J Biochem , vol.129 , pp. 835-841
    • Perrino, B.A.1    Martin, B.A.2
  • 138
    • 0034235485 scopus 로고    scopus 로고
    • Localization of a novel human A-kinase-anchoring protein, hAKAP220, during spermatogenesis
    • Reinton N., Collas P., Haugen T.B., Skalhegg B.S., Hansson V., Jahnsen T., et al. Localization of a novel human A-kinase-anchoring protein, hAKAP220, during spermatogenesis. Dev Biol 223 (2000) 194-204
    • (2000) Dev Biol , vol.223 , pp. 194-204
    • Reinton, N.1    Collas, P.2    Haugen, T.B.3    Skalhegg, B.S.4    Hansson, V.5    Jahnsen, T.6
  • 139
    • 0032528382 scopus 로고    scopus 로고
    • Regulation of recombinant PKC alpha activity by protein phosphatase 1 and protein phosphatase 2A
    • Ricciarelli R., and Azzi A. Regulation of recombinant PKC alpha activity by protein phosphatase 1 and protein phosphatase 2A. Arch Biochem Biophys 355 (1998) 197-200
    • (1998) Arch Biochem Biophys , vol.355 , pp. 197-200
    • Ricciarelli, R.1    Azzi, A.2
  • 140
    • 0028063201 scopus 로고
    • Antitumor drug fostriecin inhibits the mitotic entry checkpoint and protein phosphatases 1 and 2A
    • Roberge M., Tudan C., Hung S.M., Harder K.W., Jirik F.R., and Anderson H. Antitumor drug fostriecin inhibits the mitotic entry checkpoint and protein phosphatases 1 and 2A. Cancer Res 54 (1994) 6115-6121
    • (1994) Cancer Res , vol.54 , pp. 6115-6121
    • Roberge, M.1    Tudan, C.2    Hung, S.M.3    Harder, K.W.4    Jirik, F.R.5    Anderson, H.6
  • 141
    • 0028082299 scopus 로고
    • Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens
    • Ruediger R., Hentz M., Fait J., Mumby M., and Walter G. Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens. J Virol 68 (1994) 123-129
    • (1994) J Virol , vol.68 , pp. 123-129
    • Ruediger, R.1    Hentz, M.2    Fait, J.3    Mumby, M.4    Walter, G.5
  • 142
    • 0035853822 scopus 로고    scopus 로고
    • Multiple interactions within the AKAP220 signaling complex contribute to protein phosphatase 1 regulation
    • Schillace R.V., Voltz J.W., Sim A.T., Shenolikar S., and Scott J.D. Multiple interactions within the AKAP220 signaling complex contribute to protein phosphatase 1 regulation. J Biol Chem 276 (2001) 12128-12134
    • (2001) J Biol Chem , vol.276 , pp. 12128-12134
    • Schillace, R.V.1    Voltz, J.W.2    Sim, A.T.3    Shenolikar, S.4    Scott, J.D.5
  • 145
    • 0033458830 scopus 로고    scopus 로고
    • Targeting of PKA, PKC and protein phosphatases to cellular microdomains
    • Sim A.T., and Scott J.D. Targeting of PKA, PKC and protein phosphatases to cellular microdomains. Cell Calcium 26 (1999) 209-217
    • (1999) Cell Calcium , vol.26 , pp. 209-217
    • Sim, A.T.1    Scott, J.D.2
  • 146
    • 0028331438 scopus 로고
    • Differential activities of protein phosphatase types 1 and 2A in cytosolic and particulate fractions from rat forebrain
    • Sim A.T., Ratcliffe E., Mumby M.C., Villa-Moruzzi E., and Rostas J.A. Differential activities of protein phosphatase types 1 and 2A in cytosolic and particulate fractions from rat forebrain. J Neurochem 62 (1994) 1552-1559
    • (1994) J Neurochem , vol.62 , pp. 1552-1559
    • Sim, A.T.1    Ratcliffe, E.2    Mumby, M.C.3    Villa-Moruzzi, E.4    Rostas, J.A.5
  • 147
    • 0042068295 scopus 로고    scopus 로고
    • The role of serine/threonine protein phosphatases in exocytosis
    • Sim A.T., Baldwin M.L., Rostas J.A., Holst J., and Ludowyke R.I. The role of serine/threonine protein phosphatases in exocytosis. Biochem J 373 (2003) 641-659
    • (2003) Biochem J , vol.373 , pp. 641-659
    • Sim, A.T.1    Baldwin, M.L.2    Rostas, J.A.3    Holst, J.4    Ludowyke, R.I.5
  • 148
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: the Trojan Horse of cellular signaling
    • Sontag E. Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell Signal 13 (2001) 7-16
    • (2001) Cell Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 149
    • 5644293035 scopus 로고    scopus 로고
    • Down regulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis
    • Sontag E., Hladik C., Montgomery L., Luangpirom A., Mudrak I., Ogris E., et al. Down regulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J Neuropathol Exp Neurol 63 (2004) 1080-1091
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 1080-1091
    • Sontag, E.1    Hladik, C.2    Montgomery, L.3    Luangpirom, A.4    Mudrak, I.5    Ogris, E.6
  • 150
    • 0028153070 scopus 로고
    • Myosin reorganization in activated RBL cells correlates temporally with stimulated secretion
    • Spudich A. Myosin reorganization in activated RBL cells correlates temporally with stimulated secretion. Cell Motil Cytoskeleton 29 (1994) 345-353
    • (1994) Cell Motil Cytoskeleton , vol.29 , pp. 345-353
    • Spudich, A.1
  • 151
    • 0034683658 scopus 로고    scopus 로고
    • Recruitment of protein phosphatase 1 to the nuclear envelope by A-kinase anchoring protein AKAP149 is a prerequisite for nuclear lamina assembly
    • Steen R.L., Martins S.B., Tasken K., and Collas P. Recruitment of protein phosphatase 1 to the nuclear envelope by A-kinase anchoring protein AKAP149 is a prerequisite for nuclear lamina assembly. J Cell Biol 150 (2000) 1251-1262
    • (2000) J Cell Biol , vol.150 , pp. 1251-1262
    • Steen, R.L.1    Martins, S.B.2    Tasken, K.3    Collas, P.4
  • 152
    • 0028222312 scopus 로고
    • Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B
    • (erratum appears in Biochemistry 1995 Dec 5;34(48): 15880)
    • Stemmer P.M., and Klee C.B. Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B. (erratum appears in Biochemistry 1995 Dec 5;34(48): 15880). Biochemistry 33 (1994) 6859-6866
    • (1994) Biochemistry , vol.33 , pp. 6859-6866
    • Stemmer, P.M.1    Klee, C.B.2
  • 153
    • 0028972042 scopus 로고
    • Factors responsible for the Ca(2+)-dependent inactivation of calcineurin in brain
    • Stemmer P.M., Wang X., Krinks M.H., and Klee C.B. Factors responsible for the Ca(2+)-dependent inactivation of calcineurin in brain. FEBS Lett 374 (1995) 237-240
    • (1995) FEBS Lett , vol.374 , pp. 237-240
    • Stemmer, P.M.1    Wang, X.2    Krinks, M.H.3    Klee, C.B.4
  • 154
    • 0036830613 scopus 로고    scopus 로고
    • Overexpression of the protein phosphatase 2A regulatory subunit Bgamma promotes neuronal differentiation by activating the MAP kinase (MAPK) cascade
    • Strack S. Overexpression of the protein phosphatase 2A regulatory subunit Bgamma promotes neuronal differentiation by activating the MAP kinase (MAPK) cascade. J Biol Chem 277 (2002) 41525-41532
    • (2002) J Biol Chem , vol.277 , pp. 41525-41532
    • Strack, S.1
  • 155
    • 0032536810 scopus 로고    scopus 로고
    • Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits
    • Strack S., Zaucha J.A., Ebner F.F., Colbran R.J., and Wadzinski B.E. Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits. J Comp Neurol 392 (1998) 515-527
    • (1998) J Comp Neurol , vol.392 , pp. 515-527
    • Strack, S.1    Zaucha, J.A.2    Ebner, F.F.3    Colbran, R.J.4    Wadzinski, B.E.5
  • 156
    • 0033604321 scopus 로고    scopus 로고
    • Differential cellular and subcellular localization of protein phosphatase 1 isoforms in brain
    • Strack S., Kini S., Ebner F.F., Wadzinski B.E., and Colbran R.J. Differential cellular and subcellular localization of protein phosphatase 1 isoforms in brain. J Comp Neurol 413 (1999) 373-384
    • (1999) J Comp Neurol , vol.413 , pp. 373-384
    • Strack, S.1    Kini, S.2    Ebner, F.F.3    Wadzinski, B.E.4    Colbran, R.J.5
  • 157
    • 0037036389 scopus 로고    scopus 로고
    • Protein phosphatase 2A holoenzyme assembly: identification of contacts between B-family regulatory and scaffolding A subunits
    • Strack S., Ruediger R., Walter G., Dagda R.K., Barwacz C.A., and Cribbs J.T. Protein phosphatase 2A holoenzyme assembly: identification of contacts between B-family regulatory and scaffolding A subunits. J Biol Chem 277 (2002) 20750-20755
    • (2002) J Biol Chem , vol.277 , pp. 20750-20755
    • Strack, S.1    Ruediger, R.2    Walter, G.3    Dagda, R.K.4    Barwacz, C.A.5    Cribbs, J.T.6
  • 158
    • 0033928259 scopus 로고    scopus 로고
    • Mast cell tryptase release and asthmatic responses to allergen increase with regular use of salbutamol
    • Swystun V.A., Gordon J.R., Davis E.B., Zhang X., and Cockcroft D.W. Mast cell tryptase release and asthmatic responses to allergen increase with regular use of salbutamol. J Allergy Clin Immunol 106 (2000) 57-64
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 57-64
    • Swystun, V.A.1    Gordon, J.R.2    Davis, E.B.3    Zhang, X.4    Cockcroft, D.W.5
  • 159
    • 0034659880 scopus 로고    scopus 로고
    • Mast cell density is associated with angiogenesis and poor prognosis in pulmonary adenocarcinoma
    • Takanami I., Takeuchi K., and Naruke M. Mast cell density is associated with angiogenesis and poor prognosis in pulmonary adenocarcinoma. Cancer 88 (2000) 2686-2692
    • (2000) Cancer , vol.88 , pp. 2686-2692
    • Takanami, I.1    Takeuchi, K.2    Naruke, M.3
  • 160
    • 0027305371 scopus 로고
    • Effect of okadaic acid on histamine release from rat peritoneal mast cells activated by anti-IgE
    • Takei M., Mitsui H., and Endo K. Effect of okadaic acid on histamine release from rat peritoneal mast cells activated by anti-IgE. J Pharm Pharmacol 45 (1993) 750-752
    • (1993) J Pharm Pharmacol , vol.45 , pp. 750-752
    • Takei, M.1    Mitsui, H.2    Endo, K.3
  • 162
    • 3242694466 scopus 로고    scopus 로고
    • Involvement of filamentous actin in setting the threshold for degranulation in mast cells
    • Tolarova H., Draberova L., Heneberg P., and Draber P. Involvement of filamentous actin in setting the threshold for degranulation in mast cells. Eur J Immunol 34 (2004) 1627-1636
    • (2004) Eur J Immunol , vol.34 , pp. 1627-1636
    • Tolarova, H.1    Draberova, L.2    Heneberg, P.3    Draber, P.4
  • 163
    • 0033922452 scopus 로고    scopus 로고
    • Effect of mast cells on tumor angiogenesis in lung cancer
    • Tomita M., Matsuzaki Y., and Onitsuka T. Effect of mast cells on tumor angiogenesis in lung cancer. Ann Thorac Surg 69 (2000) 1686-1690
    • (2000) Ann Thorac Surg , vol.69 , pp. 1686-1690
    • Tomita, M.1    Matsuzaki, Y.2    Onitsuka, T.3
  • 164
    • 0035207924 scopus 로고    scopus 로고
    • Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells
    • Trinkle-Mulcahy L., Sleeman J.E., and Lamond A.I. Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci 114 (2001) 4219-4228
    • (2001) J Cell Sci , vol.114 , pp. 4219-4228
    • Trinkle-Mulcahy, L.1    Sleeman, J.E.2    Lamond, A.I.3
  • 165
    • 0028940016 scopus 로고
    • Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression
    • Turowski P., Fernandez A., Favre B., Lamb N.J., and Hemmings B.A. Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. J Cell Biol 129 (1995) 397-410
    • (1995) J Cell Biol , vol.129 , pp. 397-410
    • Turowski, P.1    Fernandez, A.2    Favre, B.3    Lamb, N.J.4    Hemmings, B.A.5
  • 166
    • 0026656413 scopus 로고
    • Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B)
    • Ueki K., Muramatsu T., and Kincaid R.L. Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B). Biochem Biophys Res Commun 187 (1992) 537-543
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 537-543
    • Ueki, K.1    Muramatsu, T.2    Kincaid, R.L.3
  • 167
    • 0033552957 scopus 로고    scopus 로고
    • Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein
    • Voorhoeve P.M., Hijmans E.M., and Bernards R. Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein. Oncogene 18 (1999) 515-524
    • (1999) Oncogene , vol.18 , pp. 515-524
    • Voorhoeve, P.M.1    Hijmans, E.M.2    Bernards, R.3
  • 168
    • 23844537784 scopus 로고    scopus 로고
    • Novel therapies for asthma-advances and problems
    • Walsh G.M. Novel therapies for asthma-advances and problems. Curr Pharm Des 11 (2005) 3027-3038
    • (2005) Curr Pharm Des , vol.11 , pp. 3027-3038
    • Walsh, G.M.1
  • 169
    • 0037647196 scopus 로고    scopus 로고
    • An overview of the protein tyrosine phosphatase superfamily
    • Wang W.Q., Sun J.P., and Zhang Z.Y. An overview of the protein tyrosine phosphatase superfamily. Curr Top Med Chem 3 (2003) 739-748
    • (2003) Curr Top Med Chem , vol.3 , pp. 739-748
    • Wang, W.Q.1    Sun, J.P.2    Zhang, Z.Y.3
  • 170
    • 0023831561 scopus 로고
    • Eosinophils and mast cells in bronchoalveolar lavage in subjects with mild asthma. Relationship to bronchial hyperreactivity
    • Wardlaw A.J., Dunnette S., Gleich G.J., Collins J.V., and Kay A.B. Eosinophils and mast cells in bronchoalveolar lavage in subjects with mild asthma. Relationship to bronchial hyperreactivity. Am Rev Respir Dis 137 (1988) 62-69
    • (1988) Am Rev Respir Dis , vol.137 , pp. 62-69
    • Wardlaw, A.J.1    Dunnette, S.2    Gleich, G.J.3    Collins, J.V.4    Kay, A.B.5
  • 171
    • 0035846951 scopus 로고    scopus 로고
    • Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p
    • Wei H., Ashby D.G., Moreno C.S., Ogris E., Yeong F.M., Corbett A.H., et al. Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. J Biol Chem 276 (2001) 1570-1577
    • (2001) J Biol Chem , vol.276 , pp. 1570-1577
    • Wei, H.1    Ashby, D.G.2    Moreno, C.S.3    Ogris, E.4    Yeong, F.M.5    Corbett, A.H.6
  • 172
    • 0033516701 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex
    • Westphal R.S., Tavalin S.J., Lin J.W., Alto N.M., Fraser I.D., Langeberg L.K., et al. Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex. Science 285 (1999) 93-96
    • (1999) Science , vol.285 , pp. 93-96
    • Westphal, R.S.1    Tavalin, S.J.2    Lin, J.W.3    Alto, N.M.4    Fraser, I.D.5    Langeberg, L.K.6
  • 173
    • 0034069624 scopus 로고    scopus 로고
    • The diverse potential effector and immunoregulatory roles of mast cells in allergic disease
    • Williams C.M., and Galli S.J. The diverse potential effector and immunoregulatory roles of mast cells in allergic disease. J Allergy Clin Immunol 105 (2000) 847-859
    • (2000) J Allergy Clin Immunol , vol.105 , pp. 847-859
    • Williams, C.M.1    Galli, S.J.2
  • 174
    • 0034618130 scopus 로고    scopus 로고
    • Mast cells can amplify airway reactivity and features of chronic inflammation in an asthma model in mice
    • Williams C.M., and Galli S.J. Mast cells can amplify airway reactivity and features of chronic inflammation in an asthma model in mice. J Exp Med 192 (2000) 455-462
    • (2000) J Exp Med , vol.192 , pp. 455-462
    • Williams, C.M.1    Galli, S.J.2
  • 175
    • 0345435932 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450
    • Witczak O., Skalhegg B.S., Keryer G., Bornens M., Tasken K., Jahnsen T., et al. Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. EMBO J 18 (1999) 1858-1868
    • (1999) EMBO J , vol.18 , pp. 1858-1868
    • Witczak, O.1    Skalhegg, B.S.2    Keryer, G.3    Bornens, M.4    Tasken, K.5    Jahnsen, T.6
  • 176
    • 0027504948 scopus 로고
    • Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction
    • Xie H., and Clarke S. Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction. J Biol Chem 268 (1993) 13364-13371
    • (1993) J Biol Chem , vol.268 , pp. 13364-13371
    • Xie, H.1    Clarke, S.2
  • 177
    • 0033972224 scopus 로고    scopus 로고
    • PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells
    • Yan Z., Fedorov S.A., Mumby M.C., and Williams R.S. PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells. Mol Cell Biol 20 (2000) 1021-1029
    • (2000) Mol Cell Biol , vol.20 , pp. 1021-1029
    • Yan, Z.1    Fedorov, S.A.2    Mumby, M.C.3    Williams, R.S.4
  • 178
    • 0034725628 scopus 로고    scopus 로고
    • Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif
    • Yang J., Hurley T.D., and DePaoli-Roach A.A. Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif. J Biol Chem 275 (2000) 22635-22644
    • (2000) J Biol Chem , vol.275 , pp. 22635-22644
    • Yang, J.1    Hurley, T.D.2    DePaoli-Roach, A.A.3
  • 179
    • 13244253758 scopus 로고    scopus 로고
    • Molecular basis for TPR domain-mediated regulation of protein phosphatase 5
    • Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., et al. Molecular basis for TPR domain-mediated regulation of protein phosphatase 5. EMBO J 24 (2005) 1-10
    • (2005) EMBO J , vol.24 , pp. 1-10
    • Yang, J.1    Roe, S.M.2    Cliff, M.J.3    Williams, M.A.4    Ladbury, J.E.5    Cohen, P.T.6
  • 180
    • 0035177048 scopus 로고    scopus 로고
    • Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen
    • Yu X.X., Du X., Moreno C.S., Green R.E., Ogris E., Feng Q., et al. Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen. Mol Biol Cell 12 (2001) 185-199
    • (2001) Mol Biol Cell , vol.12 , pp. 185-199
    • Yu, X.X.1    Du, X.2    Moreno, C.S.3    Green, R.E.4    Ogris, E.5    Feng, Q.6
  • 181
    • 11044227631 scopus 로고    scopus 로고
    • Evolution of the PPM-family protein phosphatases in Streptomyces: duplication of catalytic domain and lateral recruitment of additional sensory domains
    • Zhang W., and Shi L. Evolution of the PPM-family protein phosphatases in Streptomyces: duplication of catalytic domain and lateral recruitment of additional sensory domains. Microbiology 150 (2004) 4189-4197
    • (2004) Microbiology , vol.150 , pp. 4189-4197
    • Zhang, W.1    Shi, L.2
  • 182
    • 0037437370 scopus 로고    scopus 로고
    • Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution
    • Zhou J., Pham H.T., Ruediger R., and Walter G. Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution. Biochem J 369 (2003) 387-398
    • (2003) Biochem J , vol.369 , pp. 387-398
    • Zhou, J.1    Pham, H.T.2    Ruediger, R.3    Walter, G.4
  • 183
    • 0028879645 scopus 로고
    • Myristoylation of calcineurin B is not required for function or interaction with immunophilin-immunosuppressant complexes in the yeast Saccharomyces cerevisiae
    • Zhu D., Cardenas M.E., and Heitman J. Myristoylation of calcineurin B is not required for function or interaction with immunophilin-immunosuppressant complexes in the yeast Saccharomyces cerevisiae. J Biol Chem 270 (1995) 24831-24838
    • (1995) J Biol Chem , vol.270 , pp. 24831-24838
    • Zhu, D.1    Cardenas, M.E.2    Heitman, J.3
  • 184
    • 0034668176 scopus 로고    scopus 로고
    • Type 2A protein phosphatase, the complex regulator of numerous signaling pathways
    • Zolnierowicz S. Type 2A protein phosphatase, the complex regulator of numerous signaling pathways. Biochem Pharmacol 60 (2000) 1225-1235
    • (2000) Biochem Pharmacol , vol.60 , pp. 1225-1235
    • Zolnierowicz, S.1
  • 185
    • 0029893086 scopus 로고    scopus 로고
    • The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits
    • Zolnierowicz S., Van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., et al. The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits. Biochem J 317 (1996) 187-194
    • (1996) Biochem J , vol.317 , pp. 187-194
    • Zolnierowicz, S.1    Van Hoof, C.2    Andjelkovic, N.3    Cron, P.4    Stevens, I.5    Merlevede, W.6


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