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Volumn 9, Issue 11, 2014, Pages

Role of Ca2+and L-Phe in regulating functional cooperativity of disease-associated "toggle" calcium-sensing receptor mutations

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALCIUM SENSING RECEPTOR; INOSITOL PHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHENYLALANINE; PHOSPHOLIPASE C; CALCIUM; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 84912567710     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113622     Document Type: Article
Times cited : (19)

References (56)
  • 3
    • 0038125588 scopus 로고    scopus 로고
    • Extracellular calcium sensing and signalling
    • Hofer AM, Brown EM (2003) Extracellular calcium sensing and signalling. Nat Rev Mol Cell Biol 4: 530-538.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 530-538
    • Hofer, A.M.1    Brown, E.M.2
  • 4
    • 0036858677 scopus 로고    scopus 로고
    • L-amino acid sensing by the calcium-sensing receptor: A general mechanism for coupling protein and calcium metabolism?
    • Conigrave AD, Franks AH, Brown EM, Quinn SJ (2002) L-amino acid sensing by the calcium-sensing receptor: a general mechanism for coupling protein and calcium metabolism? Eur J Clin Nutr 56: 1072-1080.
    • (2002) Eur J Clin Nutr , vol.56 , pp. 1072-1080
    • Conigrave, A.D.1    Franks, A.H.2    Brown, E.M.3    Quinn, S.J.4
  • 5
    • 0035138842 scopus 로고    scopus 로고
    • Extracellular calcium sensing and extracellular calcium signaling
    • Brown EM, MacLeod RJ (2001) Extracellular calcium sensing and extracellular calcium signaling. Physiol Rev 81: 239-297.
    • (2001) Physiol Rev , vol.81 , pp. 239-297
    • Brown, E.M.1    MacLeod, R.J.2
  • 6
    • 33751072665 scopus 로고    scopus 로고
    • Taste receptors in the gastrointestinal tract. II. L-amino acid sensing by calcium-sensing receptors: Implications for GI physiology
    • Conigrave AD, Brown EM (2006) Taste receptors in the gastrointestinal tract. II. L-amino acid sensing by calcium-sensing receptors: implications for GI physiology. Am J Physiol Gastrointest Liver Physiol 291: G753-761.
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.291 , pp. G753-G761
    • Conigrave, A.D.1    Brown, E.M.2
  • 8
    • 21244491105 scopus 로고    scopus 로고
    • Impaired cotranslational processing of the calcium-sensing receptor due to signal peptide missense mutations in familial hypocalciuric hypercalcemia
    • Pidasheva S, Canaff L, Simonds WF, Marx SJ, Hendy GN (2005) Impaired cotranslational processing of the calcium-sensing receptor due to signal peptide missense mutations in familial hypocalciuric hypercalcemia. Hum Mol Genet 14: 1679-1690.
    • (2005) Hum Mol Genet , vol.14 , pp. 1679-1690
    • Pidasheva, S.1    Canaff, L.2    Simonds, W.F.3    Marx, S.J.4    Hendy, G.N.5
  • 9
    • 1442277000 scopus 로고    scopus 로고
    • Diseases associated with the extracellular calcium-sensing receptor
    • Thakker RV (2004) Diseases associated with the extracellular calcium-sensing receptor. Cell Calcium 35: 275-282.
    • (2004) Cell Calcium , vol.35 , pp. 275-282
    • Thakker, R.V.1
  • 10
    • 78649276821 scopus 로고    scopus 로고
    • A homozygous inactivating calcium-sensing receptor mutation, Pro339Thr, is associated with isolated primary hyperparathyroidism: Correlation between location of mutations and severity of hypercalcaemia
    • Hannan FM, Nesbit MA, Christie PT, Lissens W, Van der Schueren B, et al. (2010) A homozygous inactivating calcium-sensing receptor mutation, Pro339Thr, is associated with isolated primary hyperparathyroidism: correlation between location of mutations and severity of hypercalcaemia. Clin Endocrinol (Oxf) 73: 715-722.
    • (2010) Clin Endocrinol (Oxf) , vol.73 , pp. 715-722
    • Hannan, F.M.1    Nesbit, M.A.2    Christie, P.T.3    Lissens, W.4    Van Der Schueren, B.5
  • 12
    • 84894420817 scopus 로고    scopus 로고
    • Identification of an L-phenylalanine binding site enhancing the cooperative responses of the calcium-sensing receptor to calcium
    • Zhang C, Huang Y, Jiang Y, Mulpuri N, Wei L, et al. (2014) Identification of an L-phenylalanine binding site enhancing the cooperative responses of the calcium-sensing receptor to calcium. J Biol Chem 289: 5296-5309.
    • (2014) J Biol Chem , vol.289 , pp. 5296-5309
    • Zhang, C.1    Huang, Y.2    Jiang, Y.3    Mulpuri, N.4    Wei, L.5
  • 13
    • 84861734350 scopus 로고    scopus 로고
    • Identification of 70 calcium-sensing receptor mutations in hyper- and hypo-calcaemic patients: Evidence for clustering of extracellular domain mutations at calcium-binding sites
    • Hannan FM, Nesbit MA, Zhang C, Cranston T, Curley AJ, et al. (2012) Identification of 70 calcium-sensing receptor mutations in hyper- and hypo-calcaemic patients: evidence for clustering of extracellular domain mutations at calcium-binding sites. Hum Mol Genet 21: 2768-2778.
    • (2012) Hum Mol Genet , vol.21 , pp. 2768-2778
    • Hannan, F.M.1    Nesbit, M.A.2    Zhang, C.3    Cranston, T.4    Curley, A.J.5
  • 14
    • 0029967961 scopus 로고    scopus 로고
    • Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells
    • Pearce SH, Bai M, Quinn SJ, Kifor O, Brown EM, et al. (1996) Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells. J Clin Invest 98: 1860-1866.
    • (1996) J Clin Invest , vol.98 , pp. 1860-1866
    • Pearce, S.H.1    Bai, M.2    Quinn, S.J.3    Kifor, O.4    Brown, E.M.5
  • 15
    • 77958514966 scopus 로고    scopus 로고
    • Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1α (mGluR1α) that controls receptor activation
    • Jiang Y, Huang Y, Wong HC, Zhou Y, Wang X, et al. (2010) Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1α (mGluR1α) that controls receptor activation. J Biol Chem 285: 33463-33474.
    • (2010) J Biol Chem , vol.285 , pp. 33463-33474
    • Jiang, Y.1    Huang, Y.2    Wong, H.C.3    Zhou, Y.4    Wang, X.5
  • 16
    • 0028249912 scopus 로고
    • CLUSTAL V: Multiple alignment of DNA and protein sequences
    • Higgins DG (1994) CLUSTAL V: multiple alignment of DNA and protein sequences. Methods Mol Biol 25: 307-318.
    • (1994) Methods Mol Biol , vol.25 , pp. 307-318
    • Higgins, D.G.1
  • 17
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homologymodeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: An automated protein homologymodeling server. Nucleic Acids Res 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 20
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • Kunishima N, Shimada Y, Tsuji Y, Sato T, Yamamoto M, et al. (2000) Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407: 971-977.
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1    Shimada, Y.2    Tsuji, Y.3    Sato, T.4    Yamamoto, M.5
  • 23
    • 0029011701 scopus 로고
    • A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules
    • Cornell WD, Cieplak P, Christopher IB, Gould IR, Merz JKM, et al. (1995) A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules. J Am Chem Soc 117: 5179-5197.
    • (1995) J Am Chem Soc , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Christopher, I.B.3    Gould, I.R.4    Merz, J.K.M.5
  • 24
    • 73349094393 scopus 로고    scopus 로고
    • Reoptimization of the AMBER Force Field Parameters for Peptide Bond (Omega) Torsions Using Accelerated Molecular Dynamics
    • Urmi D, Hamelberg D (2009) Reoptimization of the AMBER Force Field Parameters for Peptide Bond (Omega) Torsions Using Accelerated Molecular Dynamics. J Phys Chem 113: 16590-16595.
    • (2009) J Phys Chem , vol.113 , pp. 16590-16595
    • Urmi, D.1    Hamelberg, D.2
  • 25
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 26
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 27
    • 0021449809 scopus 로고
    • Quasi-harmonic method for studying very low frequency modes in proteins
    • Levy RM, Srinivasan AR, Olson WK, McCammon JA (1984) Quasi-harmonic method for studying very low frequency modes in proteins. Biopolymers 23: 1099-1112.
    • (1984) Biopolymers , vol.23 , pp. 1099-1112
    • Levy, R.M.1    Srinivasan, A.R.2    Olson, W.K.3    McCammon, J.A.4
  • 28
    • 33646846296 scopus 로고    scopus 로고
    • Activation of family C G-protein-coupled receptors by the tripeptide glutathione
    • Wang M, Yao Y, Kuang D, Hampson DR (2006) Activation of family C G-protein-coupled receptors by the tripeptide glutathione. J Biol Chem 281: 8864-8870.
    • (2006) J Biol Chem , vol.281 , pp. 8864-8870
    • Wang, M.1    Yao, Y.2    Kuang, D.3    Hampson, D.R.4
  • 29
    • 0025473931 scopus 로고
    • Inositol trisphosphate analogues induce different oscillatory patterns in Xenopus oocytes
    • Berridge MJ, Potter BV (1990) Inositol trisphosphate analogues induce different oscillatory patterns in Xenopus oocytes. Cell Regul 1: 675-681.
    • (1990) Cell Regul , vol.1 , pp. 675-681
    • Berridge, M.J.1    Potter, B.V.2
  • 30
    • 0027477619 scopus 로고
    • Sinusoidal oscillations in intracellular calcium requiring negative feedback by protein kinase C
    • Bird GS, Rossier MF, Obie JF, Putney JW, Jr. (1993) Sinusoidal oscillations in intracellular calcium requiring negative feedback by protein kinase C. J Biol Chem 268: 8425-8428.
    • (1993) J Biol Chem , vol.268 , pp. 8425-8428
    • Bird, G.S.1    Rossier, M.F.2    Obie, J.F.3    Putney, J.W.4
  • 33
    • 0036014930 scopus 로고    scopus 로고
    • Aminoglycosides increase intracellular calcium levels and ERK activity in proximal tubular OK cells expressing the extracellular calcium-sensing receptor
    • Ward DT, McLarnon SJ, Riccardi D (2002) Aminoglycosides increase intracellular calcium levels and ERK activity in proximal tubular OK cells expressing the extracellular calcium-sensing receptor. J Am Soc Nephrol 13: 1481-1489.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1481-1489
    • Ward, D.T.1    McLarnon, S.J.2    Riccardi, D.3
  • 34
  • 35
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch RE, Xu K, Lewis RS (1998) Calcium oscillations increase the efficiency and specificity of gene expression. Nature 392: 933-936.
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 36
    • 0037147216 scopus 로고    scopus 로고
    • Calcium sensing receptor activation by a calcimimetic suggests a link between cooperativity and intracellular calcium oscillations
    • Miedlich S, Gama L, Breitwieser GE (2002) Calcium sensing receptor activation by a calcimimetic suggests a link between cooperativity and intracellular calcium oscillations. J Biol Chem 277: 49691-49699.
    • (2002) J Biol Chem , vol.277 , pp. 49691-49699
    • Miedlich, S.1    Gama, L.2    Breitwieser, G.E.3
  • 37
    • 33744958957 scopus 로고    scopus 로고
    • Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin
    • Huang Y, Niwa J, Sobue G, Breitwieser GE (2006) Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. J Biol Chem 281: 11610-11617.
    • (2006) J Biol Chem , vol.281 , pp. 11610-11617
    • Huang, Y.1    Niwa, J.2    Sobue, G.3    Breitwieser, G.E.4
  • 39
    • 0035001612 scopus 로고    scopus 로고
    • Regulation of MAP kinase by calcium-sensing receptor in bovine parathyroid and CaR-transfected HEK293 cells
    • Kifor O, MacLeod RJ, Diaz R, Bai M, Yamaguchi T, et al. (2001) Regulation of MAP kinase by calcium-sensing receptor in bovine parathyroid and CaR-transfected HEK293 cells. Am J Physiol Renal Physiol 280: F291-302.
    • (2001) Am J Physiol Renal Physiol , vol.280 , pp. F291-F302
    • Kifor, O.1    MacLeod, R.J.2    Diaz, R.3    Bai, M.4    Yamaguchi, T.5
  • 40
    • 0035860795 scopus 로고    scopus 로고
    • Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein
    • Awata H, Huang C, Handlogten ME, Miller RT (2001) Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein. J Biol Chem 276: 34871-34879.
    • (2001) J Biol Chem , vol.276 , pp. 34871-34879
    • Awata, H.1    Huang, C.2    Handlogten, M.E.3    Miller, R.T.4
  • 41
    • 0035860748 scopus 로고    scopus 로고
    • Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase
    • Hjalm G, MacLeod RJ, Kifor O, Chattopadhyay N, Brown EM (2001) Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase. J Biol Chem 276: 34880-34887.
    • (2001) J Biol Chem , vol.276 , pp. 34880-34887
    • Hjalm, G.1    MacLeod, R.J.2    Kifor, O.3    Chattopadhyay, N.4    Brown, E.M.5
  • 42
    • 77957821640 scopus 로고    scopus 로고
    • Naturally-occurring mutation in the calcium-sensing receptor reveals the significance of extracellular domain loop III region for class C G-protein-coupled receptor function
    • Dong Q, Cheng Z, Chang W, Blackman BE, Conte FA, et al. (2010) Naturally-occurring mutation in the calcium-sensing receptor reveals the significance of extracellular domain loop III region for class C G-protein-coupled receptor function. J Clin Endocrinol Metab 95: E245-252.
    • (2010) J Clin Endocrinol Metab , vol.95 , pp. E245-E252
    • Dong, Q.1    Cheng, Z.2    Chang, W.3    Blackman, B.E.4    Conte, F.A.5
  • 43
    • 34248139121 scopus 로고    scopus 로고
    • Rescue of calcium-sensing receptor mutants by allosteric modulators reveals a conformational checkpoint in receptor biogenesis
    • Huang Y, Breitwieser GE (2007) Rescue of calcium-sensing receptor mutants by allosteric modulators reveals a conformational checkpoint in receptor biogenesis. J Biol Chem 282: 9517-9525.
    • (2007) J Biol Chem , vol.282 , pp. 9517-9525
    • Huang, Y.1    Breitwieser, G.E.2
  • 44
    • 33745047712 scopus 로고    scopus 로고
    • Calcium sensing receptors and calcium oscillations: Calcium as a first messenger
    • Breitwieser GE (2006) Calcium sensing receptors and calcium oscillations: calcium as a first messenger. Curr Top Dev Biol 73: 85-114.
    • (2006) Curr Top Dev Biol , vol.73 , pp. 85-114
    • Breitwieser, G.E.1
  • 46
    • 0037072797 scopus 로고    scopus 로고
    • Three adjacent serines in the extracellular domains of the CaR are required for L-amino acid-mediated potentiation of receptor function
    • Zhang Z, Qiu W, Quinn SJ, Conigrave AD, Brown EM, et al. (2002) Three adjacent serines in the extracellular domains of the CaR are required for L-amino acid-mediated potentiation of receptor function. J Biol Chem 277: 33727-33735.
    • (2002) J Biol Chem , vol.277 , pp. 33727-33735
    • Zhang, Z.1    Qiu, W.2    Quinn, S.J.3    Conigrave, A.D.4    Brown, E.M.5
  • 47
    • 0037650260 scopus 로고    scopus 로고
    • The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain
    • Brauner-Osborne H, Jensen AA, Sheppard PO, O'Hara P, Krogsgaard-Larsen P (1999) The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain. J Biol Chem 274: 18382-18386.
    • (1999) J Biol Chem , vol.274 , pp. 18382-18386
    • Brauner-Osborne, H.1    Jensen, A.A.2    Sheppard, P.O.3    O'Hara, P.4    Krogsgaard-Larsen, P.5
  • 49
    • 0042233567 scopus 로고    scopus 로고
    • 2+-sensing receptor: Implications for its structure and function
    • 2+-sensing receptor: implications for its structure and function. Trends Endocrinol Metab 14: 282-288.
    • (2003) Trends Endocrinol Metab , vol.14 , pp. 282-288
    • Hu, J.1    Spiegel, A.M.2
  • 50
    • 0030724008 scopus 로고    scopus 로고
    • Identification of putative transmembrane receptor sequences homologous to the calcium-sensing G-protein-coupled receptor
    • Hinson TK, Damodaran TV, Chen J, Zhang X, Qumsiyeh MB, et al. (1997) Identification of putative transmembrane receptor sequences homologous to the calcium-sensing G-protein-coupled receptor. Genomics 45: 279-289.
    • (1997) Genomics , vol.45 , pp. 279-289
    • Hinson, T.K.1    Damodaran, T.V.2    Chen, J.3    Zhang, X.4    Qumsiyeh, M.B.5
  • 51
    • 0038125588 scopus 로고    scopus 로고
    • Extracellular calcium sensing and signalling
    • Hofer AM, Brown EM (2003) Extracellular calcium sensing and signalling. Nat Rev Mol Cell Biol 4: 530-538.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 530-538
    • Hofer, A.M.1    Brown, E.M.2
  • 53
    • 67650628028 scopus 로고    scopus 로고
    • Molecular basis for amino acid sensing by family C G-protein-coupled receptors
    • Wellendorph P, Brauner-Osborne H (2009) Molecular basis for amino acid sensing by family C G-protein-coupled receptors. Br J Pharmacol 156: 869-884.
    • (2009) Br J Pharmacol , vol.156 , pp. 869-884
    • Wellendorph, P.1    Brauner-Osborne, H.2
  • 54
    • 18144452059 scopus 로고    scopus 로고
    • 2+ requirement for high-affinity gamma-aminobutyric acid (GABA) binding at GABA(B) receptors: Involvement of serine 269 of the GABA(B)R1 subunit
    • 2+ requirement for high-affinity gamma-aminobutyric acid (GABA) binding at GABA(B) receptors: involvement of serine 269 of the GABA(B)R1 subunit. Mol Pharmacol 57: 419-426.
    • (2000) Mol Pharmacol , vol.57 , pp. 419-426
    • Galvez, T.1    Urwyler, S.2    Prezeau, L.3    Mosbacher, J.4    Joly, C.5
  • 55
    • 27844587815 scopus 로고    scopus 로고
    • 2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor
    • 2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor. J Biol Chem 280: 37917-37923.
    • (2005) J Biol Chem , vol.280 , pp. 37917-37923
    • Silve, C.1    Petrel, C.2    Leroy, C.3    Bruel, H.4    Mallet, E.5
  • 56
    • 84891442513 scopus 로고    scopus 로고
    • Two Distinct Determinants of Ligand Specificity in T1R1/T1R3 (the Umami Taste Receptor)
    • Toda Y, Nakagita T, Hayakawa T, Okada S, Narukawa M, et al. (2013) Two Distinct Determinants of Ligand Specificity in T1R1/T1R3 (the Umami Taste Receptor). J Biol Chem 288: 36863-36877.
    • (2013) J Biol Chem , vol.288 , pp. 36863-36877
    • Toda, Y.1    Nakagita, T.2    Hayakawa, T.3    Okada, S.4    Narukawa, M.5


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