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Volumn 301, Issue 3, 2011, Pages

IRAG and novel PKG targeting in the cardiovascular system

Author keywords

Guanosine 3',5' cyclic monophosphate dependent protein kinase; Inositol trisphosphate receptor associated guanosine 3',5' cyclic monophosphatekinase substrate; Nitric oxide

Indexed keywords

ACTIN; CALCIUM; CYCLIC GMP; CYCLIC GMP DEPENDENT PROTEIN KINASE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; INOSITOL TRISPHOSPHATE RECEPTOR ASSOCIATED CYCLIC GMP KINASE SUBSTRATE; MEMBRANE PROTEIN; MYOSIN; NITRIC OXIDE; UNCLASSIFIED DRUG; VASODILATOR STIMULATED PHOSPHOPROTEIN;

EID: 80052335677     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00198.2011     Document Type: Review
Times cited : (44)

References (101)
  • 1
    • 0035968197 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between the inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP kinase Ibeta
    • Ammendola A, Geiselhoringer A, Hofmann F, Schlossmann J. Molecular determinants of the interaction between the inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP kinase Ibeta. J Biol Chem 276: 24153-24159, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 24153-24159
    • Ammendola, A.1    Geiselhoringer, A.2    Hofmann, F.3    Schlossmann, J.4
  • 3
    • 0039207312 scopus 로고    scopus 로고
    • The vasodilatorstimulated phosphoprotein (VASP) is involved in cGMP-and cAMPmediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function
    • Aszodi A, Pfeifer A, Ahmad M, Glauner M, Zhou XH, Ny L, Andersson KE, Kehrel B, Offermanns S, Fassler R. The vasodilatorstimulated phosphoprotein (VASP) is involved in cGMP-and cAMPmediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function. EMBO J 18: 37-48, 1999.
    • (1999) EMBO J , vol.18 , pp. 37-48
    • Aszodi, A.1    Pfeifer, A.2    Ahmad, M.3    Glauner, M.4    Zhou, X.H.5    Ny, L.6    Andersson, K.E.7    Kehrel, B.8    Offermanns, S.9    Fassler, R.10
  • 4
    • 0025925410 scopus 로고
    • 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: A leucine/isoleucine zipper
    • Atkinson RA, Saudek V, Huggins JP, Pelton JT. 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper. Biochemistry 30: 9387-9395, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9387-9395
    • Atkinson, R.A.1    Saudek, V.2    Huggins, J.P.3    Pelton, J.T.4
  • 5
    • 36148945617 scopus 로고    scopus 로고
    • R4 RGS proteins: Regulation of G-protein signaling and beyond
    • Bansal G, Druey KM, Xie Z. R4 RGS proteins: regulation of G-protein signaling and beyond. Pharmacol Ther 116: 473-495, 2007.
    • (2007) Pharmacol Ther , vol.116 , pp. 473-495
    • Bansal, G.1    Druey, K.M.2    Xie, Z.3
  • 6
    • 46349086870 scopus 로고    scopus 로고
    • Vascular system: Role of nitric oxide in cardiovascular diseases
    • Bian K, Doursout MF, Murad F. Vascular system: role of nitric oxide in cardiovascular diseases. J Clin Hypertens (Greenwich) 10: 304-310, 2008.
    • (2008) J Clin Hypertens (Greenwich) , vol.10 , pp. 304-310
    • Bian, K.1    Doursout, M.F.2    Murad, F.3
  • 7
    • 61749096672 scopus 로고    scopus 로고
    • Modulation of cGMP in heart failure: A new therapeutic paradigm
    • Boerrigter G, Lapp H, Burnett JC. Modulation of cGMP in heart failure: a new therapeutic paradigm. Handb Exp Pharmacol 191: 485-506, 2009.
    • (2009) Handb Exp Pharmacol , vol.191 , pp. 485-506
    • Boerrigter, G.1    Lapp, H.2    Burnett, J.C.3
  • 9
    • 4043103612 scopus 로고    scopus 로고
    • Increased expression of regulator of G protein signaling-2 (RGS-2) in Bartter's/Gitelman's syndrome. A role in the control of vascular tone and implication for hypertension
    • Calo LA, Pagnin E, Davis PA, Sartori M, Ceolotto G, Pessina AC, Semplicini A. Increased expression of regulator of G protein signaling-2 (RGS-2) in Bartter's/Gitelman's syndrome. A role in the control of vascular tone and implication for hypertension. J Clin Endocrinol Metab 89: 4153-4157, 2004.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 4153-4157
    • Calo, L.A.1    Pagnin, E.2    Davis, P.A.3    Sartori, M.4    Ceolotto, G.5    Pessina, A.C.6    Semplicini, A.7
  • 10
    • 33644687046 scopus 로고    scopus 로고
    • Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif
    • Casteel DE, Boss GR, Pilz RB. Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif. J Biol Chem 280: 38211-38218, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 38211-38218
    • Casteel, D.E.1    Boss, G.R.2    Pilz, R.B.3
  • 11
    • 77958510993 scopus 로고    scopus 로고
    • A crystal structure of the cyclic GMP-dependent protein kinase Iβ dimerization/docking domain reveals molecular details of isoform-specific anchorin
    • Casteel DE, Smith-Nguyen EV, Sankaran B, Roh SH, Pilz RB, Kim C. A crystal structure of the cyclic GMP-dependent protein kinase Iβ dimerization/docking domain reveals molecular details of isoform-specific anchoring. J Biol Chem 285: 32684-32688, 2010.
    • (2010) J Biol Che , vol.28 , pp. 32684-33268
    • Casteel, D.E.1    Smith-Nguyen, E.V.2    Sankaran, B.3    Roh, S.H.4    Pilz, R.B.5    Kim, C.6
  • 12
    • 43049154714 scopus 로고    scopus 로고
    • cGMP-dependent protein kinase anchoring by IRAG regulates its nuclear translocation and transcriptional activity
    • Casteel DE, Zhang T, Zhuang S, Pilz RB. cGMP-dependent protein kinase anchoring by IRAG regulates its nuclear translocation and transcriptional activity. Cell Signal 20: 1392-1399, 2008.
    • (2008) Cell Signal , vol.20 , pp. 1392-1399
    • Casteel, D.E.1    Zhang, T.2    Zhuang, S.3    Pilz, R.B.4
  • 13
    • 78549296353 scopus 로고    scopus 로고
    • Feedback control through cGMPdependent protein kinase contributes to differential regulation and compartmentation of cGMP in rat cardiac myocytes
    • Castro LR, Schittl J, Fischmeister R. Feedback control through cGMPdependent protein kinase contributes to differential regulation and compartmentation of cGMP in rat cardiac myocytes. Circ Res 107: 1232-1240, 2010.
    • (2010) Circ Res , vol.107 , pp. 1232-1240
    • Castro, L.R.1    Schittl, J.2    Fischmeister, R.3
  • 14
    • 33846050439 scopus 로고    scopus 로고
    • LIM-only protein, CRP2, switched on smooth muscle gene activity in adult cardiac myocytes
    • Chang DF, Belaguli NS, Chang J, Schwartz RJ. LIM-only protein, CRP2, switched on smooth muscle gene activity in adult cardiac myocytes. Proc Natl Acad Sci USA 104: 157-162, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 157-162
    • Chang, D.F.1    Belaguli, N.S.2    Chang, J.3    Schwartz, R.J.4
  • 15
    • 42949095659 scopus 로고    scopus 로고
    • Atrial natriuretic peptide-initiated cGMP pathways regulate vasodilator-stimulated phosphoprotein phosphorylation and angiogenesis in vascular endothelium
    • Chen H, Levine YC, Golan DE, Michel T, Lin AJ. Atrial natriuretic peptide-initiated cGMP pathways regulate vasodilator-stimulated phosphoprotein phosphorylation and angiogenesis in vascular endothelium. J Biol Chem 283: 4439-4447, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 4439-4447
    • Chen, H.1    Levine, Y.C.2    Golan, D.E.3    Michel, T.4    Lin, A.J.5
  • 17
    • 78249272991 scopus 로고    scopus 로고
    • cGMP-dependent protein kinase and the regulation of vascular smooth muscle cell gene expression: Possible involvement of Elk-1 sumoylation
    • Choi C, Sellak H, Brown FM, Lincoln TM. cGMP-dependent protein kinase and the regulation of vascular smooth muscle cell gene expression: possible involvement of Elk-1 sumoylation. Am J Physiol Heart Circ Physiol 299: H1660-H1670, 2010.
    • (2010) Am J Physiol Heart Circ Physiol , vol.299
    • Choi, C.1    Sellak, H.2    Brown, F.M.3    Lincoln, T.M.4
  • 18
    • 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. The NO/cGMP pathway inhibits Rap 1 activation in human platelets via cGMP-dependent protein kinase I. Thromb Haemost 93: 319-325, 2005.
    • (2005) Thromb Haemost , vol.93 , pp. 319-325
    • Danielewski, O.1    Schultess, J.2    Smolenski, A.3
  • 19
    • 73949083864 scopus 로고    scopus 로고
    • VASP phosphorylation at serine239 regulates the effects of NO on smooth muscle cell invasion and contraction of collagen
    • Defawe OD, Kim S, Chen L, Huang D, Kenagy RD, Renne T, Walter U, Daum G, Clowes AW. VASP phosphorylation at serine239 regulates the effects of NO on smooth muscle cell invasion and contraction of collagen. J Cell Physiol 222: 230-237, 2010.
    • (2010) J Cell Physiol , vol.222 , pp. 230-237
    • Defawe, O.D.1    Kim, S.2    Chen, L.3    Huang, D.4    Kenagy, R.D.5    Renne, T.6    Walter, U.7    Daum, G.8    Clowes, A.W.9
  • 22
    • 77949386593 scopus 로고    scopus 로고
    • Degradation of leucine zipper-positive isoform of MYPT1 may contribute to development of nitrate tolerance
    • Dou D, Ma H, Zheng X, Ying L, Guo Y, Yu X, Gao Y. Degradation of leucine zipper-positive isoform of MYPT1 may contribute to development of nitrate tolerance. Cardiovasc Res 86: 151-159, 2010.
    • (2010) Cardiovasc Res , vol.86 , pp. 151-159
    • Dou, D.1    Ma, H.2    Zheng, X.3    Ying, L.4    Guo, Y.5    Yu, X.6    Gao, Y.7
  • 23
    • 0037805583 scopus 로고    scopus 로고
    • Serine phosphorylation negatively regulates RhoA in vivo
    • Ellerbroek SM, Wennerberg K, Burridge K. Serine phosphorylation negatively regulates RhoA in vivo. J Biol Chem 278: 19023-19031, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 19023-19031
    • Ellerbroek, S.M.1    Wennerberg, K.2    Burridge, K.3
  • 24
    • 78549231926 scopus 로고    scopus 로고
    • The role of cGMP-dependent protein kinase in controlling cardiomyocyte cGMP
    • Francis SH. The role of cGMP-dependent protein kinase in controlling cardiomyocyte cGMP. Circ Res 107: 1164-1166, 2010.
    • (2010) Circ Res , vol.107 , pp. 1164-1166
    • Francis, S.H.1
  • 26
    • 1842425000 scopus 로고    scopus 로고
    • InsP3R-associated cGMP kinase substrate (IRAG) is essential for nitric oxide-induced inhibition of calcium signaling in human colonic smooth muscle
    • Fritsch RM, Saur D, Kurjak M, Oesterle D, Schlossmann J, Geiselhoringer A, Hofmann F, Allescher HD. InsP3R-associated cGMP kinase substrate (IRAG) is essential for nitric oxide-induced inhibition of calcium signaling in human colonic smooth muscle. J Biol Chem 279: 12551-12559, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 12551-12559
    • Fritsch, R.M.1    Saur, D.2    Kurjak, M.3    Oesterle, D.4    Schlossmann, J.5    Geiselhoringer, A.6    Hofmann, F.7    Allescher, H.D.8
  • 29
    • 33846323255 scopus 로고    scopus 로고
    • MYPT1 mutants demonstrate the importance of aa 888-928 for the interaction with PKGI[1]
    • Given AM, Ogut O, Brozovich FV. MYPT1 mutants demonstrate the importance of aa 888-928 for the interaction with PKGI[1]. Am J Physiol Cell Physiol 292: C432-C439, 2007.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Given, A.M.1    Ogut, O.2    Brozovich, F.V.3
  • 30
    • 63449118167 scopus 로고    scopus 로고
    • RGS proteins: Identifying new GAPs in the understanding of blood pressure regulation and cardiovascular function
    • Gu S, Cifelli C, Wang S, Heximer SP. RGS proteins: identifying new GAPs in the understanding of blood pressure regulation and cardiovascular function. Clin Sci (Lond) 116: 391-399, 2009.
    • (2009) Clin Sci (Lond) , vol.116 , pp. 391-399
    • Gu, S.1    Cifelli, C.2    Wang, S.3    Heximer, S.P.4
  • 31
    • 0033548605 scopus 로고    scopus 로고
    • Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic nucleotidedependent kinases in vitro and in rat cerebellar slices in situ
    • Haug LS, Jensen V, Hvalby O, Walaas SI, Ostvold AC. Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic nucleotidedependent kinases in vitro and in rat cerebellar slices in situ. J Biol Chem 274: 7467-7473, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 7467-7473
    • Haug, L.S.1    Jensen, V.2    Hvalby, O.3    Walaas, S.I.4    Ostvold, A.C.5
  • 33
    • 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, Neumuller O, Danielewski O, Schultess J, Smolenski AP. Cyclic nucleotide-dependent protein kinases inhibit binding of 14-3-3 to the GTPase-activating protein Rap1GAP2 in platelets. J Biol Chem 283: 2297-2306, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 2297-2306
    • Hoffmeister, M.1    Riha, P.2    Neumuller, O.3    Danielewski, O.4    Schultess, J.5    Smolenski, A.P.6
  • 36
    • 33644834949 scopus 로고    scopus 로고
    • Function of cGMPdependent protein kinases as revealed by gene deletion
    • Hofmann F, Feil R, Kleppisch T, Schlossmann J. Function of cGMPdependent protein kinases as revealed by gene deletion. Physiol Rev 86: 1-23, 2006.
    • (2006) Physiol Rev , vol.86 , pp. 1-23
    • Hofmann, F.1    Feil, R.2    Kleppisch, T.3    Schlossmann, J.4
  • 37
    • 0034007868 scopus 로고    scopus 로고
    • Cysteine-rich protein 2, a novel substrate for cGMP kinase I in enteric neurons and intestinal smooth muscle
    • Huber A, Neuhuber WL, Klugbauer N, Ruth P, Allescher HD. Cysteine-rich protein 2, a novel substrate for cGMP kinase I in enteric neurons and intestinal smooth muscle. J Biol Chem 275: 5504-5511, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 5504-5511
    • Huber, A.1    Neuhuber, W.L.2    Klugbauer, N.3    Ruth, P.4    Allescher, H.D.5
  • 45
    • 0025037397 scopus 로고
    • Effects of cyclic GMP on the secondary structure of cyclic GMP dependent protein kinase and analysis of the enzyme's amino-terminal domain by far-ultraviolet circular dichroism
    • Landgraf W, Hofmann F, Pelton JT, Huggins JP. Effects of cyclic GMP on the secondary structure of cyclic GMP dependent protein kinase and analysis of the enzyme's amino-terminal domain by far-ultraviolet circular dichroism. Biochemistry 29: 9921-9928, 1990.
    • (1990) Biochemistry , vol.29 , pp. 9921-9928
    • Landgraf, W.1    Hofmann, F.2    Pelton, J.T.3    Huggins, J.P.4
  • 46
    • 0026080004 scopus 로고
    • Oxidation of cysteines activates cGMP-dependent protein kinase
    • Landgraf W, Regulla S, Meyer HE, Hofmann F. Oxidation of cysteines activates cGMP-dependent protein kinase. J Biol Chem 266: 16305-16311, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 16305-16311
    • Landgraf, W.1    Regulla, S.2    Meyer, H.E.3    Hofmann, F.4
  • 47
    • 35148819200 scopus 로고    scopus 로고
    • Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase
    • Lee E, Hayes DB, Langsetmo K, Sundberg EJ, Tao TC. Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase. J Mol Biol 373: 1198-1212, 2007.
    • (2007) J Mol Biol , vol.373 , pp. 1198-1212
    • Lee, E.1    Hayes, D.B.2    Langsetmo, K.3    Sundberg, E.J.4    Tao, T.C.5
  • 48
    • 73449132939 scopus 로고    scopus 로고
    • Evaluation of differentially expressed genes identified in keratoconus
    • Lee JE, Oum BS, Choi HY, Lee SU, Lee JS. Evaluation of differentially expressed genes identified in keratoconus. Mol Vis 15: 2480-2487, 2009.
    • (2009) Mol Vis , vol.15 , pp. 2480-2487
    • Lee, J.E.1    Oum, B.S.2    Choi, H.Y.3    Lee, S.U.4    Lee, J.S.5
  • 49
    • 34948857998 scopus 로고    scopus 로고
    • Modulation of lamellipodial structure and dynamics by NO-dependent phosphorylation of VASP Ser239
    • Lindsay SL, Ramsey S, Aitchison M, Renne T, Evans TJ. Modulation of lamellipodial structure and dynamics by NO-dependent phosphorylation of VASP Ser239. J Cell Sci 120: 3011-3021, 2007.
    • (2007) J Cell Sci , vol.120 , pp. 3011-3021
    • Lindsay, S.L.1    Ramsey, S.2    Aitchison, M.3    Renne, T.4    Evans, T.J.5
  • 50
    • 77953508462 scopus 로고    scopus 로고
    • Increased degradation of MYPT1 contributes to the development of tolerance to nitric oxide in porcine pulmonary artery
    • Ma H, He Q, Dou D, Zheng X, Ying L, Wu Y, Raj JU, Gao Y. Increased degradation of MYPT1 contributes to the development of tolerance to nitric oxide in porcine pulmonary artery. Am J Physiol Lung Cell Mol Physiol 299: L117-L123, 2010.
    • (2010) Am J Physiol Lung Cell Mol Physiol , vol.299
    • Ma, H.1    He, Q.2    Dou, D.3    Zheng, X.4    Ying, L.5    Wu, Y.6    Raj, J.U.7    Gao, Y.8
  • 53
    • 78549237861 scopus 로고    scopus 로고
    • InsP3R-associated cGMP kinase substrate determines inositol 1,4,5-trisphosphate receptor susceptibility to phosphoregulation by cyclic nucleotide-dependent kinases
    • Masuda W, Betzenhauser MJ, Yule DI. InsP3R-associated cGMP kinase substrate determines inositol 1,4,5-trisphosphate receptor susceptibility to phosphoregulation by cyclic nucleotide-dependent kinases. J Biol Chem 285: 37927-37938, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 37927-37938
    • Masuda, W.1    Betzenhauser, M.J.2    Yule, D.I.3
  • 55
    • 33645547231 scopus 로고    scopus 로고
    • NO-sensitive guanylyl cyclase and NO-induced feedback inhibition in cGMP signaling
    • Mullershausen F, Koesling D, Friebe A. NO-sensitive guanylyl cyclase and NO-induced feedback inhibition in cGMP signaling. Front Biosci 10: 1269-1278, 2005.
    • (2005) Front Biosci , vol.10 , pp. 1269-1278
    • Mullershausen, F.1    Koesling, D.2    Friebe, A.3
  • 56
    • 0037571979 scopus 로고    scopus 로고
    • Inhibition of sustained smooth muscle contraction by PKA and PKG preferentially mediated by phosphorylation of RhoA
    • Murthy KS, Zhou H, Grider JR, Makhlouf GM. Inhibition of sustained smooth muscle contraction by PKA and PKG preferentially mediated by phosphorylation of RhoA. Am J Physiol Gastrointest Liver Physiol 284: G1006-G1016, 2003.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.284
    • Murthy, K.S.1    Zhou, H.2    Grider, J.R.3    Makhlouf, G.M.4
  • 60
    • 35748984127 scopus 로고    scopus 로고
    • Regulation of RGS2 and second messenger signaling in vascular smooth muscle cells by cGMP-dependent protein kinase
    • Osei-Owusu P, Sun X, Drenan RM, Steinberg TH, Blumer KJ. Regulation of RGS2 and second messenger signaling in vascular smooth muscle cells by cGMP-dependent protein kinase. J Biol Chem 282: 31656-31665, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 31656-31665
    • Osei-Owusu, P.1    Sun, X.2    Drenan, R.M.3    Steinberg, T.H.4    Blumer, K.J.5
  • 61
    • 0034903134 scopus 로고    scopus 로고
    • Expression of RGS3, RGS4 and Gi alpha 2 in acutely failing donor hearts and end-stage heart failure
    • Owen VJ, Burton PB, Mullen AJ, Birks EJ, Barton P, Yacoub MH. Expression of RGS3, RGS4 and Gi alpha 2 in acutely failing donor hearts and end-stage heart failure. Eur Heart J 22: 1015-1020, 2001.
    • (2001) Eur Heart J , vol.22 , pp. 1015-1020
    • Owen, V.J.1    Burton, P.B.2    Mullen, A.J.3    Birks, E.J.4    Barton, P.5    Yacoub, M.H.6
  • 64
    • 0346118927 scopus 로고    scopus 로고
    • Dimerization of cGMPdependent protein kinase Ibeta is mediated by an extensive aminoterminal leucine zipper motif, and dimerization modulates enzyme function
    • Richie-Jannetta R, Francis SH, Corbin JD. Dimerization of cGMPdependent protein kinase Ibeta is mediated by an extensive aminoterminal leucine zipper motif, and dimerization modulates enzyme function. J Biol Chem 278: 50070-50079, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 50070-50079
    • Richie-Jannetta, R.1    Francis, S.H.2    Corbin, J.D.3
  • 66
    • 20444480169 scopus 로고    scopus 로고
    • Phosphorylation of serine 188 protects RhoA from ubiquitin/proteasome-mediated degradation in vascular smooth muscle cells
    • Rolli-Derkinderen M, Sauzeau V, Boyer L, Lemichez E, Baron C, Henrion D, Loirand G, Pacaud P. Phosphorylation of serine 188 protects RhoA from ubiquitin/proteasome-mediated degradation in vascular smooth muscle cells. Circ Res 96: 1152-1160, 2005.
    • (2005) Circ Res , vol.96 , pp. 1152-1160
    • Rolli-Derkinderen, M.1    Sauzeau, V.2    Boyer, L.3    Lemichez, E.4    Baron, C.5    Henrion, D.6    Loirand, G.7    Pacaud, P.8
  • 68
    • 0036479319 scopus 로고    scopus 로고
    • Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells
    • Rybalkin SD, Rybalkina IG, Feil R, Hofmann F, Beavo JA. Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells. J Biol Chem 277: 3310-3317, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 3310-3317
    • Rybalkin, S.D.1    Rybalkina, I.G.2    Feil, R.3    Hofmann, F.4    Beavo, J.A.5
  • 73
    • 79954563422 scopus 로고    scopus 로고
    • Signaling via IRAG is essential for NO/cGMP-dependent inhibition of platelet activation
    • Schinner E, Salb K, Schlossmann J. Signaling via IRAG is essential for NO/cGMP-dependent inhibition of platelet activation. Platelets 22: 217-227, 2011.
    • (2011) Platelets , vol.22 , pp. 217-227
    • Schinner, E.1    Salb, K.2    Schlossmann, J.3
  • 77
    • 24344487878 scopus 로고    scopus 로고
    • Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: Application to cGMP-dependent protein kinase Ialpha
    • Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ. Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha. Protein Sci 14: 2421-2428, 2005.
    • (2005) Protein Sci , vol.14 , pp. 2421-2428
    • Schnell, J.R.1    Zhou, G.P.2    Zweckstetter, M.3    Rigby, A.C.4    Chou, J.J.5
  • 78
    • 17044406762 scopus 로고    scopus 로고
    • Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets
    • Schultess J, Danielewski O, Smolenski AP. Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets. Blood 105: 3185-3192, 2005.
    • (2005) Blood , vol.105 , pp. 3185-3192
    • Schultess, J.1    Danielewski, O.2    Smolenski, A.P.3
  • 79
    • 57749112083 scopus 로고    scopus 로고
    • Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase
    • Sharma AK, Zhou GP, Kupferman J, Surks HK, Christensen EN, Chou JJ, Mendelsohn ME, Rigby AC. Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase. J Biol Chem 283: 32860-32869, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 32860-32869
    • Sharma, A.K.1    Zhou, G.P.2    Kupferman, J.3    Surks, H.K.4    Christensen, E.N.5    Chou, J.J.6    Mendelsohn, M.E.7    Rigby, A.C.8
  • 80
    • 0033602316 scopus 로고    scopus 로고
    • Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a protein with homology to a lymphoidrestricted membrane protein Jaw1
    • Shaughnessy JD Jr, Largaespada DA, Tian E, Fletcher CF, Cho BC, Vyas P, Jenkins NA, Copeland NG. Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a protein with homology to a lymphoidrestricted membrane protein Jaw1. Oncogene 18: 2069-2084, 1999.
    • (1999) Oncogene , vol.18 , pp. 2069-2084
    • Shaughnessy Jr., J.D.1    Largaespada, D.A.2    Tian, E.3    Fletcher, C.F.4    Cho, B.C.5    Vyas, P.6    Jenkins, N.A.7    Copeland, N.G.8
  • 81
    • 48049116208 scopus 로고    scopus 로고
    • Proteolytic processing of cGMP-dependent protein kinase I mediates nuclear cGMP signaling in vascular smooth muscle cells
    • Sugiura T, Nakanishi H, Roberts JD Jr. Proteolytic processing of cGMP-dependent protein kinase I mediates nuclear cGMP signaling in vascular smooth muscle cells. Circ Res 103: 53-60, 2008.
    • (2008) Circ Res , vol.103 , pp. 53-60
    • Sugiura, T.1    Nakanishi, H.2    Roberts Jr., J.D.3
  • 82
    • 14944383669 scopus 로고    scopus 로고
    • RGS2 is a mediator of nitric oxide action on blood pressure and vasoconstrictor signaling
    • Sun X, Kaltenbronn KM, Steinberg TH, Blumer KJ. RGS2 is a mediator of nitric oxide action on blood pressure and vasoconstrictor signaling. Mol Pharmacol 67: 631-639, 2005.
    • (2005) Mol Pharmacol , vol.67 , pp. 631-639
    • Sun, X.1    Kaltenbronn, K.M.2    Steinberg, T.H.3    Blumer, K.J.4
  • 87
    • 0242580679 scopus 로고    scopus 로고
    • Phosphorylation of type-1 inositol 1,4,5-trisphosphate receptors by cyclic nucleotide-dependent protein kinases: A mutational analysis of the functionally important sites in the S2+ and S2-splice variants
    • Wagner LE 2nd, Li WH, Yule DI. Phosphorylation of type-1 inositol 1,4,5-trisphosphate receptors by cyclic nucleotide-dependent protein kinases: a mutational analysis of the functionally important sites in the S2+ and S2-splice variants. J Biol Chem 278: 45811-45817, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 45811-45817
    • Wagner II, L.E.1    Li, W.H.2    Yule, D.I.3
  • 89
    • 2642514777 scopus 로고    scopus 로고
    • Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells
    • Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME. Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells. J Biol Chem 279: 24420-24426, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 24420-24426
    • Wang, Y.1    El-Zaru, M.R.2    Surks, H.K.3    Mendelsohn, M.E.4
  • 91
    • 45449098668 scopus 로고    scopus 로고
    • Differential regulation of RhoA-mediated signaling by the TPalpha and TPbeta isoforms of the human thromboxane A2 receptor: Independent modulation of TPalpha signaling by prostacyclin and nitric oxide
    • Wikstrom K, Kavanagh DJ, Reid HM, Kinsella BT. Differential regulation of RhoA-mediated signaling by the TPalpha and TPbeta isoforms of the human thromboxane A2 receptor: independent modulation of TPalpha signaling by prostacyclin and nitric oxide. Cell Signal 20: 1497-1512, 2008.
    • (2008) Cell Signal , vol.20 , pp. 1497-1512
    • Wikstrom, K.1    Kavanagh, D.J.2    Reid, H.M.3    Kinsella, B.T.4
  • 92
    • 51649121968 scopus 로고    scopus 로고
    • Compartmentation and compartment-specific regulation of PDE5 by protein kinase G allows selective cGMP-mediated regulation of platelet functions
    • Wilson LS, Elbatarny HS, Crawley SW, Bennett BM, Maurice DH. Compartmentation and compartment-specific regulation of PDE5 by protein kinase G allows selective cGMP-mediated regulation of platelet functions. Proc Natl Acad Sci USA 105: 13650-13655, 2008.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13650-13655
    • Wilson, L.S.1    Elbatarny, H.S.2    Crawley, S.W.3    Bennett, B.M.4    Maurice, D.H.5
  • 94
    • 4544321243 scopus 로고    scopus 로고
    • Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides
    • Wooldridge AA, MacDonald JA, Erdodi F, Ma C, Borman MA, Hartshorne DJ, Haystead TA. Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides. J Biol Chem 279: 34496-34504, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 34496-34504
    • Wooldridge, A.A.1    Macdonald, J.A.2    Erdodi, F.3    Ma, C.4    Borman, M.A.5    Hartshorne, D.J.6    Haystead, T.A.7
  • 97
    • 77957265020 scopus 로고    scopus 로고
    • Functional osteoclast attachment requires inositol-1,4,5-trisphosphate receptor-associated cGMP-dependent kinase substrate
    • Yaroslavskiy BB, Turkova I, Wang Y, Robinson LJ, Blair HC. Functional osteoclast attachment requires inositol-1,4,5-trisphosphate receptor-associated cGMP-dependent kinase substrate. Lab Invest 90: 1533-1542, 2010.
    • (2010) Lab Invest , vol.90 , pp. 1533-1542
    • Yaroslavskiy, B.B.1    Turkova, I.2    Wang, Y.3    Robinson, L.J.4    Blair, H.C.5
  • 98
    • 0033601333 scopus 로고    scopus 로고
    • A novel interaction of cGMP-dependent protein kinase I with troponin T
    • Yuasa K, Michibata H, Omori K, Yanaka N. A novel interaction of cGMP-dependent protein kinase I with troponin T. J Biol Chem 274: 37429-37434, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37429-37434
    • Yuasa, K.1    Michibata, H.2    Omori, K.3    Yanaka, N.4
  • 99
    • 36348939376 scopus 로고    scopus 로고
    • A cysteine-rich LIM-only protein mediates regulation of smooth musclespecific gene expression by cGMP-dependent protein kinase
    • Zhang T, Zhuang S, Casteel DE, Looney DJ, Boss GR, Pilz RB. A cysteine-rich LIM-only protein mediates regulation of smooth musclespecific gene expression by cGMP-dependent protein kinase. J Biol Chem 282: 33367-33380, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 33367-33380
    • Zhang, T.1    Zhuang, S.2    Casteel, D.E.3    Looney, D.J.4    Boss, G.R.5    Pilz, R.B.6


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