메뉴 건너뛰기




Volumn 49, Issue 22, 2010, Pages 4601-4610

Role of juxtamembrane and transmembrane domains in the mechanism of natriuretic peptide receptor a activation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE RESIDUES; ATRIAL NATRIURETIC PEPTIDES; BEFORE AND AFTER; CONFORMATIONAL CHANGE; CRYSTALLOGRAPHIC STUDIES; CYSTEINE RESIDUES; EXPERIMENTAL DATA; EXTRACELLULAR DOMAINS; GUANYLYL CYCLASE; INTRACELLULAR DOMAIN; JUXTAMEMBRANE DOMAINS; LIGAND-BINDING SITES; MOLECULAR MODELS; NATRIURETIC PEPTIDE RECEPTOR A; NONCOVALENT; ROTATION MECHANISM; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANE DOMAIN; TRANSMEMBRANES;

EID: 77953090807     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901711w     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 32444444836 scopus 로고    scopus 로고
    • Natriuretic peptides, their receptors, and cyclic guanosine monophosphate-dependent signaling functions
    • Potter, L. R., Abbey-Hosch, S., and Dickey, D. M. (2006) Natriuretic peptides, their receptors, and cyclic guanosine monophosphate-dependent signaling functions Endocr. Rev. 27, 47-72
    • (2006) Endocr. Rev. , vol.27 , pp. 47-72
    • Potter, L.R.1    Abbey-Hosch, S.2    Dickey, D.M.3
  • 2
    • 33847042749 scopus 로고    scopus 로고
    • Molecular biology of the natriuretic peptide system: Implications for physiology and hypertension
    • Gardner, D. G., Chen, S., Glenn, D. J., and Grigsby, C. L. (2007) Molecular biology of the natriuretic peptide system: Implications for physiology and hypertension Hypertension 49, 419-426
    • (2007) Hypertension , vol.49 , pp. 419-426
    • Gardner, D.G.1    Chen, S.2    Glenn, D.J.3    Grigsby, C.L.4
  • 3
    • 0842342073 scopus 로고    scopus 로고
    • Molecular physiology of natriuretic peptide signalling
    • Kuhn, M. (2004) Molecular physiology of natriuretic peptide signalling Basic Res. Cardiol. 99, 76-82
    • (2004) Basic Res. Cardiol. , vol.99 , pp. 76-82
    • Kuhn, M.1
  • 4
    • 10444270958 scopus 로고    scopus 로고
    • The use of recombinant human B-type natriuretic peptide (nesiritide) in the management of acute decompensated heart failure
    • Strain, W. D. (2004) The use of recombinant human B-type natriuretic peptide (nesiritide) in the management of acute decompensated heart failure Int. J. Clin. Pract. 58, 1081-1087
    • (2004) Int. J. Clin. Pract. , vol.58 , pp. 1081-1087
    • Strain, W.D.1
  • 5
    • 34250358937 scopus 로고    scopus 로고
    • Natriuretic peptides and therapeutic applications
    • Lee, C. Y. and Burnett, J. C., Jr. (2007) Natriuretic peptides and therapeutic applications Heart Failure Rev. 12, 131-142
    • (2007) Heart Failure Rev. , vol.12 , pp. 131-142
    • Lee, C.Y.1    Burnett Jr., J.C.2
  • 6
    • 58049211379 scopus 로고    scopus 로고
    • Novel bifunctional natriuretic peptides as potential therapeutics
    • Dickey, D. M., Burnett, J. C., Jr., and Potter, L. R. (2008) Novel bifunctional natriuretic peptides as potential therapeutics J. Biol. Chem. 283, 35003-35009
    • (2008) J. Biol. Chem. , vol.283 , pp. 35003-35009
    • Dickey, D.M.1    Burnett Jr., J.C.2    Potter, L.R.3
  • 7
    • 77953084271 scopus 로고    scopus 로고
    • Discovery of a Novel Synthetic Natriuretic Peptide, CU-NP
    • Lee, C. Y. W. and Burnett, J. C., Jr. (2007) Discovery of a Novel Synthetic Natriuretic Peptide, CU-NP J. Card. Failure 13, S74
    • (2007) J. Card. Failure , vol.13 , pp. 74
    • Lee, C.Y.W.1    Burnett Jr., J.C.2
  • 8
    • 7044233148 scopus 로고    scopus 로고
    • Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases
    • Padayatti, P. S., Pattanaik, P., Ma, X., and van den Akker, F. (2004) Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases Pharmacol. Ther. 104, 83-99
    • (2004) Pharmacol. Ther. , vol.104 , pp. 83-99
    • Padayatti, P.S.1    Pattanaik, P.2    Ma, X.3    Van Den Akker, F.4
  • 9
    • 0028965963 scopus 로고
    • Stoichiometry of the atrial natriuretic factor-R1 receptor complex in the bovine zona glomerulosa
    • Rondeau, J. J., McNicoll, N., Gagnon, J., Bouchard, N., Ong, H., and De Lean, A. (1995) Stoichiometry of the atrial natriuretic factor-R1 receptor complex in the bovine zona glomerulosa Biochemistry 34, 2130-2136
    • (1995) Biochemistry , vol.34 , pp. 2130-2136
    • Rondeau, J.J.1    McNicoll, N.2    Gagnon, J.3    Bouchard, N.4    Ong, H.5    De Lean, A.6
  • 10
    • 0025994797 scopus 로고
    • Allosteric modulation by ATP of the bovine adrenal natriuretic factor R1 receptor functions
    • Larose, L., McNicoll, N., Ong, H., and De Lean, A. (1991) Allosteric modulation by ATP of the bovine adrenal natriuretic factor R1 receptor functions Biochemistry 30, 8990-8995
    • (1991) Biochemistry , vol.30 , pp. 8990-8995
    • Larose, L.1    McNicoll, N.2    Ong, H.3    De Lean, A.4
  • 11
    • 19544376001 scopus 로고    scopus 로고
    • ATP-regulated module (ARM) of the atrial natriuretic factor receptor guanylate cyclase
    • Duda, T., Venkataraman, V., Ravichandran, S., and Sharma, R. K. (2005) ATP-regulated module (ARM) of the atrial natriuretic factor receptor guanylate cyclase Peptides 26, 969-984
    • (2005) Peptides , vol.26 , pp. 969-984
    • Duda, T.1    Venkataraman, V.2    Ravichandran, S.3    Sharma, R.K.4
  • 12
    • 0024461962 scopus 로고
    • The protein kinase domain of the ANP receptor is required for signaling
    • Chinkers, M. and Garbers, D. L. (1989) The protein kinase domain of the ANP receptor is required for signaling Science 245, 1392-1394
    • (1989) Science , vol.245 , pp. 1392-1394
    • Chinkers, M.1    Garbers, D.L.2
  • 13
    • 27644591220 scopus 로고    scopus 로고
    • Atrial natriuretic peptide-dependent photolabeling of a regulatory ATP-binding site on the natriuretic peptide receptor-A
    • Joubert, S., Jossart, C., McNicoll, N., and De Lean, A. (2005) Atrial natriuretic peptide-dependent photolabeling of a regulatory ATP-binding site on the natriuretic peptide receptor-A FEBS J. 272, 5572-5583
    • (2005) FEBS J. , vol.272 , pp. 5572-5583
    • Joubert, S.1    Jossart, C.2    McNicoll, N.3    De Lean, A.4
  • 14
    • 0035909101 scopus 로고    scopus 로고
    • Reduced activity of the NPR-A kinase triggers dephosphorylation and homologous desensitization of the receptor
    • Joubert, S., Labrecque, J., and De Lean, A. (2001) Reduced activity of the NPR-A kinase triggers dephosphorylation and homologous desensitization of the receptor Biochemistry 40, 11096-11105
    • (2001) Biochemistry , vol.40 , pp. 11096-11105
    • Joubert, S.1    Labrecque, J.2    De Lean, A.3
  • 15
    • 33847111062 scopus 로고    scopus 로고
    • Biochemical and pharmacological characterization of P-site inhibitors on homodimeric guanylyl cyclase domain from natriuretic peptide receptor-A
    • Joubert, S., McNicoll, N., and De Lean, A. (2007) Biochemical and pharmacological characterization of P-site inhibitors on homodimeric guanylyl cyclase domain from natriuretic peptide receptor-A Biochem. Pharmacol. 73, 954-963
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 954-963
    • Joubert, S.1    McNicoll, N.2    De Lean, A.3
  • 16
    • 0033592859 scopus 로고    scopus 로고
    • Ligand binding-dependent limited proteolysis of the atrial natriuretic peptide receptor: Juxtamembrane hinge structure essential for transmembrane signal transduction
    • Huo, X., Abe, T., and Misono, K. S. (1999) Ligand binding-dependent limited proteolysis of the atrial natriuretic peptide receptor: Juxtamembrane hinge structure essential for transmembrane signal transduction Biochemistry 38, 16941-16951
    • (1999) Biochemistry , vol.38 , pp. 16941-16951
    • Huo, X.1    Abe, T.2    Misono, K.S.3
  • 17
    • 0040736351 scopus 로고    scopus 로고
    • A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity. Role of receptor dimerization in signal transduction
    • Labrecque, J., Mc Nicoll, N., Marquis, M., and De Lean, A. (1999) A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity. Role of receptor dimerization in signal transduction J. Biol. Chem. 274, 9752-9759
    • (1999) J. Biol. Chem. , vol.274 , pp. 9752-9759
    • Labrecque, J.1    Mc Nicoll, N.2    Marquis, M.3    De Lean, A.4
  • 18
    • 0035896533 scopus 로고    scopus 로고
    • Agonistic induction of a covalent dimer in a mutant of natriuretic peptide receptor-A documents a juxtamembrane interaction that accompanies receptor activation
    • Labrecque, J., Deschenes, J., McNicoll, N., and De Lean, A. (2001) Agonistic induction of a covalent dimer in a mutant of natriuretic peptide receptor-A documents a juxtamembrane interaction that accompanies receptor activation J. Biol. Chem. 276, 8064-8072
    • (2001) J. Biol. Chem. , vol.276 , pp. 8064-8072
    • Labrecque, J.1    Deschenes, J.2    McNicoll, N.3    De Lean, A.4
  • 19
    • 38549143915 scopus 로고    scopus 로고
    • Role of extracellular domain dimerization in agonist-induced activation of natriuretic peptide receptor A
    • Parat, M., McNicoll, N., Wilkes, B., Fournier, A., and De Lean, A. (2008) Role of extracellular domain dimerization in agonist-induced activation of natriuretic peptide receptor A Mol. Pharmacol. 73, 431-440
    • (2008) Mol. Pharmacol. , vol.73 , pp. 431-440
    • Parat, M.1    McNicoll, N.2    Wilkes, B.3    Fournier, A.4    De Lean, A.5
  • 20
    • 3142582002 scopus 로고    scopus 로고
    • Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: Rotation mechanism for transmembrane signal transduction
    • Ogawa, H., Qiu, Y., Ogata, C. M., and Misono, K. S. (2004) Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: Rotation mechanism for transmembrane signal transduction J. Biol. Chem. 279, 28625-28631
    • (2004) J. Biol. Chem. , vol.279 , pp. 28625-28631
    • Ogawa, H.1    Qiu, Y.2    Ogata, C.M.3    Misono, K.S.4
  • 22
    • 0033786730 scopus 로고    scopus 로고
    • Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase
    • Bell, C. A., Tynan, J. A., Hart, K. C., Meyer, A. N., Robertson, S. C., and Donoghue, D. J. (2000) Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase Mol. Biol. Cell 11, 3589-3599
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3589-3599
    • Bell, C.A.1    Tynan, J.A.2    Hart, K.C.3    Meyer, A.N.4    Robertson, S.C.5    Donoghue, D.J.6
  • 23
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T., Maruyama, H., and Maruyama, I. N. (2001) Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain J. Mol. Biol. 311, 1011-1026
    • (2001) J. Mol. Biol. , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 24
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • Lu, X., Gross, A. W., and Lodish, H. F. (2006) Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains J. Biol. Chem. 281, 7002-7011
    • (2006) J. Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 26
    • 0024319129 scopus 로고
    • Distinct properties of atrial natriuretic factor receptor subpopulations in epithelial and fibroblast cell lines
    • Fethiere, J., Meloche, S., Nguyen, T. T., Ong, H., and De Lean, A. (1989) Distinct properties of atrial natriuretic factor receptor subpopulations in epithelial and fibroblast cell lines Mol. Pharmacol. 35, 584-592
    • (1989) Mol. Pharmacol. , vol.35 , pp. 584-592
    • Fethiere, J.1    Meloche, S.2    Nguyen, T.T.3    Ong, H.4    De Lean, A.5
  • 27
    • 0026777809 scopus 로고
    • Dephosphorylation of the guanylyl cyclase-A receptor causes desensitization
    • Potter, L. R. and Garbers, D. L. (1992) Dephosphorylation of the guanylyl cyclase-A receptor causes desensitization J. Biol. Chem. 267, 14531-14534
    • (1992) J. Biol. Chem. , vol.267 , pp. 14531-14534
    • Potter, L.R.1    Garbers, D.L.2
  • 28
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D., Brosig, B., Kolmar, H., and Fritz, H. J. (1996) Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator J. Mol. Biol. 263, 525-530
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 29
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar, H., Hennecke, F., Gotze, K., Janzer, B., Vogt, B., Mayer, F., and Fritz, H. J. (1995) Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures EMBO J. 14, 3895-3904
    • (1995) EMBO J. , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Hennecke, F.2    Gotze, K.3    Janzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.J.7
  • 30
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • Brosig, B. and Langosch, D. (1998) The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues Protein Sci. 7, 1052-1056
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 31
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 33
    • 3242878412 scopus 로고    scopus 로고
    • 3DCoffee@igs: A web server for combining sequences and structures into a multiple sequence alignment
    • Poirot, O., Suhre, K., Abergel, C., O'Toole, E., and Notredame, C. (2004) 3DCoffee@igs: A web server for combining sequences and structures into a multiple sequence alignment Nucleic Acids Res. 32, W37-W40
    • (2004) Nucleic Acids Res. , vol.32
    • Poirot, O.1    Suhre, K.2    Abergel, C.3    O'Toole, E.4    Notredame, C.5
  • 34
    • 0034612573 scopus 로고    scopus 로고
    • Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor
    • van den Akker, F., Zhang, X., Miyagi, M., Huo, X., Misono, K. S., and Yee, V. C. (2000) Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor Nature 406, 101-104
    • (2000) Nature , vol.406 , pp. 101-104
    • Van Den Akker, F.1    Zhang, X.2    Miyagi, M.3    Huo, X.4    Misono, K.S.5    Yee, V.C.6
  • 35
    • 0018001339 scopus 로고
    • Simultaneous analysis of families of sigmoidal curves: Application to bioassay, radioligand assay, and physiological dose-response curves
    • DeLean, A., Munson, P. J., and Rodbard, D. (1978) Simultaneous analysis of families of sigmoidal curves: Application to bioassay, radioligand assay, and physiological dose-response curves Am. J. Physiol. 235, E97-E102
    • (1978) Am. J. Physiol. , vol.235
    • Delean, A.1    Munson, P.J.2    Rodbard, D.3
  • 37
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann, K. M., Xiao, W., Shin, Y. K., and Koshland, D. E., Jr. (1999) A piston model for transmembrane signaling of the aspartate receptor Science 285, 1751-1754
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland Jr., D.E.4
  • 38
    • 0033615077 scopus 로고    scopus 로고
    • Receptor signaling: When dimerization is not enough
    • Jiang, G. and Hunter, T. (1999) Receptor signaling: When dimerization is not enough Curr. Biol. 9, R568-R571
    • (1999) Curr. Biol. , vol.9
    • Jiang, G.1    Hunter, T.2
  • 39
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I. A., and Michnick, S. W. (1999) Erythropoietin receptor activation by a ligand-induced conformation change Science 283, 990-993
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 40
    • 0031842104 scopus 로고    scopus 로고
    • Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
    • Burke, C. L. and Stern, D. F. (1998) Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface Mol. Cell. Biol. 18, 5371-5379
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5371-5379
    • Burke, C.L.1    Stern, D.F.2
  • 42
    • 0026725829 scopus 로고
    • Ligand-independent oligomerization of natriuretic peptide receptors. Identification of heteromeric receptors and a dominant negative mutant
    • Chinkers, M. and Wilson, E. M. (1992) Ligand-independent oligomerization of natriuretic peptide receptors. Identification of heteromeric receptors and a dominant negative mutant J. Biol. Chem. 267, 18589-18597
    • (1992) J. Biol. Chem. , vol.267 , pp. 18589-18597
    • Chinkers, M.1    Wilson, E.M.2
  • 43
    • 0031195159 scopus 로고    scopus 로고
    • Hydrophobic forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrane mimetic surface: An NMR study
    • Carpenter, K. A., Wilkes, B. C., De Lean, A., Fournier, A., and Schiller, P. W. (1997) Hydrophobic forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrane mimetic surface: An NMR study Biopolymers 42, 37-48
    • (1997) Biopolymers , vol.42 , pp. 37-48
    • Carpenter, K.A.1    Wilkes, B.C.2    De Lean, A.3    Fournier, A.4    Schiller, P.W.5
  • 44
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka, B. K. and Deupi, X. (2007) Conformational complexity of G-protein-coupled receptors Trends Pharmacol. Sci. 28, 397-406
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.