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Volumn 71, Issue 1, 1998, Pages 248-257

Pertussis toxin modification of PC12 cells inhibits a protein phosphatase 2A-like phosphatase

Author keywords

Calcineurin; G Proteins; PC12 cells; Pertussis toxin; Protein phosphatase 2A

Indexed keywords

PERTUSSIS TOXIN; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A;

EID: 0031866371     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71010248.x     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 0023522389 scopus 로고
    • 2+-stimulated catecholamine release from α-toxin-permeabilized PC12 cells: Biochemical evidence for exocytosis and its modulation by protein kinase C and G proteins
    • 2+-stimulated catecholamine release from α-toxin-permeabilized PC12 cells: biochemical evidence for exocytosis and its modulation by protein kinase C and G proteins. Biochemistry 26, 7842-7848.
    • (1987) Biochemistry , vol.26 , pp. 7842-7848
    • Ahnert-Hilger, G.1    Brautigam, M.2    Gratzl, M.3
  • 3
    • 0027055668 scopus 로고
    • Role of heterotrimeric G proteins in membrane traffic
    • Bomsel M. and Mostov K. (1992) Role of heterotrimeric G proteins in membrane traffic. Mol. Biol. Cell 3, 1317-1328.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1317-1328
    • Bomsel, M.1    Mostov, K.2
  • 4
    • 0025157815 scopus 로고
    • Hydrolysis resistant GTP analogs stimulate catecholamine release from digitonin-permeabilized PC12 cells
    • Carroll A. G., Rhoads A. R., and Wagner P. D. (1990) Hydrolysis resistant GTP analogs stimulate catecholamine release from digitonin-permeabilized PC12 cells. J. Neurochem. 55, 930-936.
    • (1990) J. Neurochem. , vol.55 , pp. 930-936
    • Carroll, A.G.1    Rhoads, A.R.2    Wagner, P.D.3
  • 5
    • 0028241170 scopus 로고
    • 14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation
    • Chen F. and Wagner P. D. (1994) 14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation. FEBS Lett. 347, 128-132.
    • (1994) FEBS Lett. , vol.347 , pp. 128-132
    • Chen, F.1    Wagner, P.D.2
  • 6
    • 0030702944 scopus 로고    scopus 로고
    • Pertussis toxin modification of PC12 cells lowers cytoskeletal F-actin and enhances norepinephrine secretion: Involvement of protein kinase C and protein phosphatases
    • Chen F. and Wagner P. D. (1997) Pertussis toxin modification of PC12 cells lowers cytoskeletal F-actin and enhances norepinephrine secretion: involvement of protein kinase C and protein phosphatases. Arch. Physiol. Biochem. 105, 317-328.
    • (1997) Arch. Physiol. Biochem. , vol.105 , pp. 317-328
    • Chen, F.1    Wagner, P.D.2
  • 7
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • Chen J., Martin B. L., and Brautigan D. L. (1992) Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science 257, 1261-1264.
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 8
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58, 453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 9
    • 0024361302 scopus 로고
    • An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues
    • Cohen P., Klumpp S., and Schelling D. L. (1989) An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues. FEBS Lett. 250, 596-600.
    • (1989) FEBS Lett. , vol.250 , pp. 596-600
    • Cohen, P.1    Klumpp, S.2    Schelling, D.L.3
  • 10
    • 0026062464 scopus 로고
    • Dopaminergic regulation of dopamine release from PC12 cells via a pertussis toxin-sensitive G protein
    • Courtney N. D., Howlett A. C., and Westfall T. C. (1991) Dopaminergic regulation of dopamine release from PC12 cells via a pertussis toxin-sensitive G protein. Neurosci. Lett. 122, 261-264.
    • (1991) Neurosci. Lett. , vol.122 , pp. 261-264
    • Courtney, N.D.1    Howlett, A.C.2    Westfall, T.C.3
  • 12
    • 0026503434 scopus 로고
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A
    • Fruman D. A., Klee C. B., Bierer B. E., and Burakoff S. J. (1992) Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A. Proc. Natl. Acad. Sci. USA 89, 3686-3690.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3686-3690
    • Fruman, D.A.1    Klee, C.B.2    Bierer, B.E.3    Burakoff, S.J.4
  • 13
    • 0026764957 scopus 로고
    • Chromostatin inhibits catecholamine secretion in adrenal chromaffin cells by activating a protein phosphatase
    • Galindo E., Zwiller J., Bader M-F., and Aunis D. (1992) Chromostatin inhibits catecholamine secretion in adrenal chromaffin cells by activating a protein phosphatase. Proc. Natl. Acad. Sci. USA 89, 7398-7402.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7398-7402
    • Galindo, E.1    Zwiller, J.2    Bader, M.-F.3    Aunis, D.4
  • 15
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman A. G. (1987) G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 16
    • 0027477103 scopus 로고
    • Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A
    • Guo H. and Damuni Z. (1993) Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A. Proc. Natl. Acad. Sci. USA 90, 2500-2504.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2500-2504
    • Guo, H.1    Damuni, Z.2
  • 17
    • 0025898450 scopus 로고
    • Identification, purification, and characterization of a novel serine/threonine protein phosphatase from bovine brain
    • Honkanen R. E., Zwiller J., Daily S. L., Charter B. S., Dukelow M., and Boynton A. L. (1991) Identification, purification, and characterization of a novel serine/threonine protein phosphatase from bovine brain. J. Biol. Chem. 266, 6614-6619.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6614-6619
    • Honkanen, R.E.1    Zwiller, J.2    Daily, S.L.3    Charter, B.S.4    Dukelow, M.5    Boynton, A.L.6
  • 18
    • 0028826397 scopus 로고
    • Angiotensin II type 2 receptor-mediated stimulation of protein phosphatase 2A in rat hypothalamic/brainstem neuronal cocultures
    • Huang X.-C., Richards E. M., and Summers C. (1995) Angiotensin II type 2 receptor-mediated stimulation of protein phosphatase 2A in rat hypothalamic/brainstem neuronal cocultures. J. Neurochem. 65, 2131-2137.
    • (1995) J. Neurochem. , vol.65 , pp. 2131-2137
    • Huang, X.-C.1    Richards, E.M.2    Summers, C.3
  • 19
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities
    • Ingebritsen T. S. and Cohen P. (1983) The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem. 132, 255-261.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 20
    • 0031031397 scopus 로고    scopus 로고
    • HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint
    • Kawabe T., Muslin A. J., and Korsmeyer S. J. (1997) HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint. Nature 385, 454-457.
    • (1997) Nature , vol.385 , pp. 454-457
    • Kawabe, T.1    Muslin, A.J.2    Korsmeyer, S.J.3
  • 21
    • 0025910365 scopus 로고
    • Structure and function of signal-transducing GTP-binding proteins
    • Kaziro Y., Itoh I., Kozasa T., Nakafuku M., and Satoh T. (1991) Structure and function of signal-transducing GTP-binding proteins. Annu. Rev. Biochem. 60, 349-400.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 349-400
    • Kaziro, Y.1    Itoh, I.2    Kozasa, T.3    Nakafuku, M.4    Satoh, T.5
  • 22
    • 0029665228 scopus 로고    scopus 로고
    • PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 35, 6998-7002.
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 23
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li M., Makkinje A., and Damuni Z. (1996b) The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 271, 11059-11062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 24
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., Farmer J. D. Jr., Lane W. S., Friedman J., Weissman I., and Schreiber S. L. (1991) Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 26
    • 0023882060 scopus 로고
    • Calmodulinand protein phosphorylation-independent release of catecholamine from PC-12 cells
    • Matthies H. J. G., Palfrey H. C, and Miller R. J. (1988) Calmodulinand protein phosphorylation-independent release of catecholamine from PC-12 cells. FEBS Lett. 229, 238-242.
    • (1988) FEBS Lett. , vol.229 , pp. 238-242
    • Matthies, H.J.G.1    Palfrey, H.C.2    Miller, R.J.3
  • 27
    • 0026729258 scopus 로고
    • Maitotoxin-induced intracellular calcium rise in PC12 cells: Involvement of dihydropyridine-sensitive and w-conotoxin-sensitive calcium channels and phosphoinositide breakdown
    • Meucci O., Grimaldi M., Scorziello A., Govoni S., Bergamaschi S., Yasumoto T., and Schettini G. (1992) Maitotoxin-induced intracellular calcium rise in PC12 cells: involvement of dihydropyridine-sensitive and w-conotoxin-sensitive calcium channels and phosphoinositide breakdown. J. Neurochem. 59, 679-688.
    • (1992) J. Neurochem. , vol.59 , pp. 679-688
    • Meucci, O.1    Grimaldi, M.2    Scorziello, A.3    Govoni, S.4    Bergamaschi, S.5    Yasumoto, T.6    Schettini, G.7
  • 30
    • 0024644539 scopus 로고
    • A comparison of bradykinin, angiotensin II and muscarinic stimulation of cultured bovine chromaffin cells
    • O'Sullivan A. J. and Burgoyne R. D. (1989) A comparison of bradykinin, angiotensin II and muscarinic stimulation of cultured bovine chromaffin cells. Biosci. Rep. 9, 243-252.
    • (1989) Biosci. Rep. , vol.9 , pp. 243-252
    • O'Sullivan, A.J.1    Burgoyne, R.D.2
  • 31
    • 0026682699 scopus 로고
    • G protein activation of a hormone-stimulated phosphatase in human tumor cells
    • Pan M. G., Florio T., and Stork P. J. (1992) G protein activation of a hormone-stimulated phosphatase in human tumor cells. Science 256, 1215-1217.
    • (1992) Science , vol.256 , pp. 1215-1217
    • Pan, M.G.1    Florio, T.2    Stork, P.J.3
  • 32
    • 0023932685 scopus 로고
    • Calcium/calmodulin-dependent protein kinase. II: Characterization of distinct calmodulin binding and inhibitory domains
    • Payne M. E., Fong Y.-L., Ono T., Colbran R. J., Kemp B. E., Soderling T. R., and Means A. R. (1988) Calcium/calmodulin-dependent protein kinase. II: Characterization of distinct calmodulin binding and inhibitory domains. J. Biol. Chem. 263, 7190-7195.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7190-7195
    • Payne, M.E.1    Fong, Y.-L.2    Ono, T.3    Colbran, R.J.4    Kemp, B.E.5    Soderling, T.R.6    Means, A.R.7
  • 33
    • 0022838615 scopus 로고
    • 2+, ATP, and protein kinase C activators
    • 2+, ATP, and protein kinase C activators. J. Biol. Chem. 261, 14665-14669.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14665-14669
    • Peppers, S.C.1    Holz, R.W.2
  • 34
    • 0027379383 scopus 로고
    • ATP-induced secretion in PC12 cells and photoaffinity labeling of receptors
    • Rhoads A. R., Paru R., Vu N.-D., Cadogan R., and Wagner P. D. (1993) ATP-induced secretion in PC12 cells and photoaffinity labeling of receptors. J. Neurochem. 61, 1657-1666.
    • (1993) J. Neurochem. , vol.61 , pp. 1657-1666
    • Rhoads, A.R.1    Paru, R.2    Vu, N.-D.3    Cadogan, R.4    Wagner, P.D.5
  • 35
    • 0023939860 scopus 로고
    • 2+ mobilization and inositol triphosphate formation in cultured adrenal chromaffin cells
    • 2+ mobilization and inositol triphosphate formation in cultured adrenal chromaffin cells. Biochem. Pharmacol. 37, 2485-2487.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 2485-2487
    • Sasakawa, N.1    Yamamoto, S.2    Nakaki, T.3    Kato, R.4
  • 36
    • 0021284158 scopus 로고
    • Protein (serine and threonine) phosphate phosphatases
    • Shenolikar S. and Ingebritsen T. S. (1984) Protein (serine and threonine) phosphate phosphatases. Methods Enzymol. 107, 102-129.
    • (1984) Methods Enzymol. , vol.107 , pp. 102-129
    • Shenolikar, S.1    Ingebritsen, T.S.2
  • 37
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation
    • Sontag E., Fedorov S., Kamibayashi C., Robbins D., Cobb M., and Mumby M. (1993) The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation. Cell 75, 887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 38
    • 0026019306 scopus 로고
    • A pertussis-toxin-sensitive protein controls exocytosis in chromaffin cells at a step distal to the generation of second messengers
    • Sontag J.-M., Thierse D., Rouot B., Aunis D., and Bader M.-F. (1991) A pertussis-toxin-sensitive protein controls exocytosis in chromaffin cells at a step distal to the generation of second messengers. Biochem. J. 274, 339-347.
    • (1991) Biochem. J. , vol.274 , pp. 339-347
    • Sontag, J.-M.1    Thierse, D.2    Rouot, B.3    Aunis, D.4    Bader, M.-F.5
  • 39
    • 0024324350 scopus 로고
    • Muscarinic-stimulated norepinephrine release and phosphoinositide hydrolysis in PC12 cells are independent events
    • Takashima A. and Kenimer A. G. (1989) Muscarinic-stimulated norepinephrine release and phosphoinositide hydrolysis in PC12 cells are independent events. J. Biol. Chem. 264, 10654-10659.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10654-10659
    • Takashima, A.1    Kenimer, A.G.2
  • 40
    • 0023182146 scopus 로고
    • Pertussis toxin facilitates secretagogue-induced catecholamine release from cultured bovine adrenal chromaffin cells
    • Tanaka T., Yokohama H., Negishi M., Hayashi H., Ito S., and Hayaishi O. (1987) Pertussis toxin facilitates secretagogue-induced catecholamine release from cultured bovine adrenal chromaffin cells. Biochem. Biophys. Res. Commun. 144, 907-914.
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 907-914
    • Tanaka, T.1    Yokohama, H.2    Negishi, M.3    Hayashi, H.4    Ito, S.5    Hayaishi, O.6
  • 41
    • 0003085965 scopus 로고
    • Pertussis toxin as a valuable probe for G-protein involvement in signal transduction
    • (Moss J., and Vaughan M., eds), American Society of Microbiology, Washington, D.C.
    • Ui M. (1990) Pertussis toxin as a valuable probe for G-protein involvement in signal transduction, in ADP-Ribosylating Toxins and G Proteins (Moss J., and Vaughan M., eds), pp. 45-77. American Society of Microbiology, Washington, D.C.
    • (1990) ADP-Ribosylating Toxins and G Proteins , pp. 45-77
    • Ui, M.1
  • 42
    • 0028302133 scopus 로고
    • Exocytosis in chromaffin cells: Evidence for a MgATP-independent step that requires a pertussis toxin-sensitive GTP-binding protein
    • Vitale N., Thierse D., Aunis D., and Bader M.-F. (1994) Exocytosis in chromaffin cells: evidence for a MgATP-independent step that requires a pertussis toxin-sensitive GTP-binding protein. Biochem. J. 300, 217-227.
    • (1994) Biochem. J. , vol.300 , pp. 217-227
    • Vitale, N.1    Thierse, D.2    Aunis, D.3    Bader, M.-F.4
  • 44
    • 0027244764 scopus 로고
    • Protein serine/threonine phosphatases and cell transformation
    • Walter G. and Mumby M. (1993) Protein serine/threonine phosphatases and cell transformation. Biochim. Biophys. Acta 1155, 207-226.
    • (1993) Biochim. Biophys. Acta , vol.1155 , pp. 207-226
    • Walter, G.1    Mumby, M.2


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