메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; CYCLIC NUCLEOTIDE; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN 14 3 3; PROTEIN ANTIBODY; RGS PROTEIN; RGS18 PROTEIN; SERINE; SPINOPHILIN; THROMBIN; THROMBOXANE A2; UNCLASSIFIED DRUG; RGS18 PROTEIN, HUMAN;

EID: 84892380287     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080251     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 84856512481 scopus 로고    scopus 로고
    • Novel roles of cAMP/cGMP dependent signaling in platelets
    • Smolenski A (2011) Novel roles of cAMP/cGMP dependent signaling in platelets. Journal of Thrombosis and Haemostasis 10: 167-176.
    • (2011) Journal of Thrombosis and Haemostasis , vol.10 , pp. 167-176
    • Smolenski, A.1
  • 3
    • 33846187547 scopus 로고    scopus 로고
    • IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation
    • Antl M, von Bruehl M-L, Eiglsperger C, Werner M, Konrad I, et al. (2007) IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood 109: 552-559.
    • (2007) Blood , vol.109 , pp. 552-559
    • Antl, M.1    Von Bruehl, M.-L.2    Eiglsperger, C.3    Werner, M.4    Konrad, I.5
  • 4
    • 0028303913 scopus 로고
    • cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets
    • Butt E, Abel K, Krieger M, Palm D, Hoppe V, et al. (1994) cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. Journal of Biological Chemistry 269: 14509-14517.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 14509-14517
    • Butt, E.1    Abel, K.2    Krieger, M.3    Palm, D.4    Hoppe, V.5
  • 5
    • 0032493663 scopus 로고    scopus 로고
    • Analysis and Regulation of Vasodilator-stimulated Phosphoprotein Serine 239 Phosphorylation in Vitro and in Intact Cells Using a Phosphospecific Monoclonal Antibody
    • Smolenski A, Bachmann C, Reinhard K, Hoenig-Liedl P, Jarchau T, et al. (1998) Analysis and Regulation of Vasodilator-stimulated Phosphoprotein Serine 239 Phosphorylation in Vitro and in Intact Cells Using a Phosphospecific Monoclonal Antibody. Journal of Biological Chemistry 273: 20029-20035.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 20029-20035
    • Smolenski, A.1    Bachmann, C.2    Reinhard, K.3    Hoenig-Liedl, P.4    Jarchau, T.5
  • 6
    • 17044406762 scopus 로고    scopus 로고
    • Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets
    • Schultess J, Danielewski O, Smolenski AP (2005) Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets. Blood 105: 3185-3192.
    • (2005) Blood , vol.105 , pp. 3185-3192
    • Schultess, J.1    Danielewski, O.2    Smolenski, A.P.3
  • 8
    • 84879027082 scopus 로고    scopus 로고
    • Phosphorylation of the guanine-nucleotide-exchange factor CalDAG-GEFI by protein kinase A regulates Ca(2+)-dependent activation of platelet Rap1b GTPase
    • Guidetti GF, Manganaro D, Consonni A, Canobbio I, Balduini C, et al. (2013) Phosphorylation of the guanine-nucleotide-exchange factor CalDAG-GEFI by protein kinase A regulates Ca(2+)-dependent activation of platelet Rap1b GTPase. Biochem J 453: 115-123.
    • (2013) Biochem J , vol.453 , pp. 115-123
    • Guidetti, G.F.1    Manganaro, D.2    Consonni, A.3    Canobbio, I.4    Balduini, C.5
  • 9
    • 84860340490 scopus 로고    scopus 로고
    • Regulator of G-protein signaling 18 integrates activating and inhibitory signaling in platelets
    • Gegenbauer K, Elia G, Blanco-Fernandez A, Smolenski A (2012) Regulator of G-protein signaling 18 integrates activating and inhibitory signaling in platelets. Blood 119: 3799-3807.
    • (2012) Blood , vol.119 , pp. 3799-3807
    • Gegenbauer, K.1    Elia, G.2    Blanco-Fernandez, A.3    Smolenski, A.4
  • 11
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • Siderovski DP, Willard FS (2005) The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits. Int J Biol Sci 1: 51-66.
    • (2005) Int J Biol Sci , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 12
    • 79961071855 scopus 로고    scopus 로고
    • Genome wide RNA-seq analysis of human and mouse platelet transcriptomes
    • Rowley JW, Oler A, Tolley ND, Hunter B, Low EN, et al. (2011) Genome wide RNA-seq analysis of human and mouse platelet transcriptomes. Blood 118: e101-111.
    • (2011) Blood , vol.118
    • Rowley, J.W.1    Oler, A.2    Tolley, N.D.3    Hunter, B.4    Low, E.N.5
  • 13
    • 84867754221 scopus 로고    scopus 로고
    • The first comprehensive and quantitative analysis of human platelet protein composition allows the comparative analysis of structural and functional pathways
    • Epub ahead of print
    • Burkhart JM, Vaudel M, Gambaryan S, Radau S, Walter U, et al. (2012) The first comprehensive and quantitative analysis of human platelet protein composition allows the comparative analysis of structural and functional pathways. Blood: Epub ahead of print.
    • (2012) Blood
    • Burkhart, J.M.1    Vaudel, M.2    Gambaryan, S.3    Radau, S.4    Walter, U.5
  • 14
    • 84868115018 scopus 로고    scopus 로고
    • Regulators of g protein signaling (RGS): Role in hematopoiesis, megakaryopoiesis and platelet function
    • Epub ahead of print
    • Louwette S, Van Geet C, Freson K (2012) Regulators of g protein signaling (RGS): role in hematopoiesis, megakaryopoiesis and platelet function. Journal of Thrombosis and Haemostasis: Epub ahead of print.
    • (2012) Journal of Thrombosis and Haemostasis
    • Louwette, S.1    Van Geet, C.2    Freson, K.3
  • 15
    • 84860899306 scopus 로고    scopus 로고
    • Regulator of G-protein signaling 18 controls megakaryopoiesis and the cilia-mediated vertebrate mechanosensory system
    • Louwette S, Labarque V, Wittevrongel C, Thys C, Metz J, et al. (2012) Regulator of G-protein signaling 18 controls megakaryopoiesis and the cilia-mediated vertebrate mechanosensory system. FASEB J 26: 2125-2136.
    • (2012) FASEB J , vol.26 , pp. 2125-2136
    • Louwette, S.1    Labarque, V.2    Wittevrongel, C.3    Thys, C.4    Metz, J.5
  • 16
    • 0036223127 scopus 로고    scopus 로고
    • Cloning and characterization of a novel regulator of G protein signalling in human platelets
    • Gagnon AW, Murray DL, Leadley RJ (2002) Cloning and characterization of a novel regulator of G protein signalling in human platelets. Cellular Signalling 14: 595-606.
    • (2002) Cellular Signalling , vol.14 , pp. 595-606
    • Gagnon, A.W.1    Murray, D.L.2    Leadley, R.J.3
  • 17
    • 0035847017 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells
    • Park IK, Klug CA, Li K, Jerabek L, Li L, et al. (2001) Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells. J Biol Chem 276: 915-923.
    • (2001) J Biol Chem , vol.276 , pp. 915-923
    • Park, I.K.1    Klug, C.A.2    Li, K.3    Jerabek, L.4    Li, L.5
  • 18
    • 84868115018 scopus 로고    scopus 로고
    • Regulators of G protein signaling: Role in hematopoiesis, megakaryopoiesis and platelet function
    • Louwette S, Van Geet C, Freson K (2012) Regulators of G protein signaling: role in hematopoiesis, megakaryopoiesis and platelet function. Journal of Thrombosis and Haemostasis 10: 2215-2222.
    • (2012) Journal of Thrombosis and Haemostasis , vol.10 , pp. 2215-2222
    • Louwette, S.1    Van Geet, C.2    Freson, K.3
  • 19
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G, Avruch J (2002) 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem 277: 3061-3064.
    • (2002) J Biol Chem , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 20
    • 70350340056 scopus 로고    scopus 로고
    • Serine/Threonine Phosphatases: Mechanism through Structure
    • Shi Y (2009) Serine/Threonine Phosphatases: Mechanism through Structure. Cell 139: 468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 21
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen PTW (2002) Protein phosphatase 1 - targeted in many directions. Journal of Cell Science 115: 241-256.
    • (2002) Journal of Cell Science , vol.115 , pp. 241-256
    • Cohen, P.T.W.1
  • 22
    • 84872769362 scopus 로고    scopus 로고
    • The PP1 binding code: A molecular-lego strategy that governs specificity
    • Heroes E, Lesage B, Görnemann J, Beullens M, Van Meervelt L, et al. (2013) The PP1 binding code: a molecular-lego strategy that governs specificity. FEBS Journal 280: 584-595.
    • (2013) FEBS Journal , vol.280 , pp. 584-595
    • Heroes, E.1    Lesage, B.2    Görnemann, J.3    Beullens, M.4    Van Meervelt, L.5
  • 24
    • 0033528669 scopus 로고    scopus 로고
    • Characterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1†
    • Hsieh-Wilson LC, Allen PB, Watanabe T, Nairn AC, Greengard P (1999) Characterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1†. Biochemistry 38: 4365-4373.
    • (1999) Biochemistry , vol.38 , pp. 4365-4373
    • Hsieh-Wilson, L.C.1    Allen, P.B.2    Watanabe, T.3    Nairn, A.C.4    Greengard, P.5
  • 25
    • 13844276837 scopus 로고    scopus 로고
    • The NO/cGMP pathway inhibits Rap 1 activation in human platelets via cGMP-dependent protein kinase I
    • Danielewski O, Schultess J, Smolenski A (2005) The NO/cGMP pathway inhibits Rap 1 activation in human platelets via cGMP-dependent protein kinase I. Thromb Haemost 93: 319-325.
    • (2005) Thromb Haemost , vol.93 , pp. 319-325
    • Danielewski, O.1    Schultess, J.2    Smolenski, A.3
  • 26
    • 33344470872 scopus 로고    scopus 로고
    • C-terminal binding: An expanded repertoire and function of 14-3-3 proteins
    • Coblitz B, Wu M, Shikano S, Li M (2006) C-terminal binding: An expanded repertoire and function of 14-3-3 proteins. FEBS Letters 580: 1531-1535.
    • (2006) FEBS Letters , vol.580 , pp. 1531-1535
    • Coblitz, B.1    Wu, M.2    Shikano, S.3    Li, M.4
  • 27
    • 0031470652 scopus 로고    scopus 로고
    • The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
    • Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, et al. (1997) The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity. Cell 91: 961-971.
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1    Rittinger, K.2    Volinia, S.3    Caron, P.R.4    Aitken, A.5
  • 28
    • 12144289394 scopus 로고    scopus 로고
    • Differential proteome analysis of TRAP-activated platelets: Involvement of DOK-2 and phosphorylation of RGS proteins
    • Garcia A, Prabhakar S, Hughan S, Anderson TW, Brock CJ, et al. (2004) Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins. Blood 103: 2088-2095.
    • (2004) Blood , vol.103 , pp. 2088-2095
    • Garcia, A.1    Prabhakar, S.2    Hughan, S.3    Anderson, T.W.4    Brock, C.J.5
  • 29
    • 84857520121 scopus 로고    scopus 로고
    • A newly-identified complex of spinophilin and the tyrosine phosphatase, SHP-1, modulates platelet activation by regulating G protein-dependent signaling
    • Ma P, Cierniewska A, Signarvic R, Cieslak M, Kong H, et al. (2011) A newly-identified complex of spinophilin and the tyrosine phosphatase, SHP-1, modulates platelet activation by regulating G protein-dependent signaling. Blood 119: 1935-1945.
    • (2011) Blood , vol.119 , pp. 1935-1945
    • Ma, P.1    Cierniewska, A.2    Signarvic, R.3    Cieslak, M.4    Kong, H.5
  • 30
    • 47649124124 scopus 로고    scopus 로고
    • A Global View of Gene Activity and Alternative Splicing by Deep Sequencing of the Human Transcriptome
    • Sultan M, Schulz MH, Richard H, Magen A, Klingenhoff A, et al. (2008) A Global View of Gene Activity and Alternative Splicing by Deep Sequencing of the Human Transcriptome. Science 321: 956-960.
    • (2008) Science , vol.321 , pp. 956-960
    • Sultan, M.1    Schulz, M.H.2    Richard, H.3    Magen, A.4    Klingenhoff, A.5
  • 33
    • 77950519767 scopus 로고    scopus 로고
    • Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
    • Ragusa MJ, Dancheck B, Critton DA, Nairn AC, Page R, et al. (2010) Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat Struct Mol Biol 17: 459-464.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 459-464
    • Ragusa, M.J.1    Dancheck, B.2    Critton, D.A.3    Nairn, A.C.4    Page, R.5
  • 34
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins
    • Waterman MJ, Stavridi ES, Waterman JL, Halazonetis TD (1998) ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins. Nat Genet 19: 175-178.
    • (1998) Nat Genet , vol.19 , pp. 175-178
    • Waterman, M.J.1    Stavridi, E.S.2    Waterman, J.L.3    Halazonetis, T.D.4
  • 35
    • 38349174744 scopus 로고    scopus 로고
    • Cyclic Nucleotide-dependent Protein Kinases Inhibit Binding of 14-3-3 to the GTPase-activating Protein Rap1GAP2 in Platelets
    • Hoffmeister M, Riha P, Neumüller O, Danielewski O, Schultess J, et al. (2008) Cyclic Nucleotide-dependent Protein Kinases Inhibit Binding of 14-3-3 to the GTPase-activating Protein Rap1GAP2 in Platelets. Journal of Biological Chemistry 283: 2297-2306.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 2297-2306
    • Hoffmeister, M.1    Riha, P.2    Neumüller, O.3    Danielewski, O.4    Schultess, J.5
  • 37
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis SS, Walsh S, Weiser DC, Yoshida M, Shenolikar S, et al. (2003) PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J 22: 5734-5745.
    • (2003) EMBO J , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Weiser, D.C.3    Yoshida, M.4    Shenolikar, S.5
  • 38
    • 78049391231 scopus 로고    scopus 로고
    • Mitotic Phosphorylation of Cdc25B Ser321 Disrupts 14-3-3 Binding to the High Affinity Ser323 Site
    • Astuti P, Boutros R, Ducommun B, Gabrielli B (2010) Mitotic Phosphorylation of Cdc25B Ser321 Disrupts 14-3-3 Binding to the High Affinity Ser323 Site. Journal of Biological Chemistry 285: 34364-34370.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 34364-34370
    • Astuti, P.1    Boutros, R.2    Ducommun, B.3    Gabrielli, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.