[ad_1]
Brown, E. M. et al. Cloning and characterization of an extracellular Ca2+-sensing receptor from bovine parathyroid. Nature 366, 575–580 (1993).
Hofer, A. M. & Brown, E. M. Extracellular calcium sensing and signalling. Nat. Rev. Mol. Cell Biol. 4, 530–538 (2003).
Gray, E. et al. Activation of the extracellular calcium-sensing receptor initiates insulin secretion from human islets of Langerhans: involvement of protein kinases. J. Endocrinol. 190, 703–710 (2006).
Mace, O. J., Schindler, M. & Patel, S. The regulation of K- and L-cell activity by GLUT2 and the calcium-sensing receptor CasR in rat small intestine. J. Physiol. 590, 2917–2936 (2012).
Ruat, M. & Traiffort, E. Roles of the calcium sensing receptor in the central nervous system. Best Pract. Res. Clin. Endocrinol. Metab. 27, 429–442 (2013).
Conigrave, A. D. & Ward, D. T. Calcium-sensing receptor (CaSR): pharmacological properties and signaling pathways. Best Pract. Res. Clin. Endocrinol. Metab. 27, 315–331 (2013).
Hendy, G. N., Guarnieri, V. & Canaff, L. Calcium-sensing receptor and associated diseases. Prog. Mol. Biol. Transl. Sci. 89, 31–95 (2009).
de Jesus Ferreira, M. C. et al. Co-expression of a Ca2+-inhibitable adenylyl cyclase and of a Ca2+-sensing receptor in the cortical thick ascending limb cell of the rat kidney. Inhibition of hormone-dependent cAMP accumulation by extracellular Ca2+. J. Biol. Chem. 273, 15192–15202 (1998).
Kifor, O. et al. Regulation of MAP kinase by calcium-sensing receptor in bovine parathyroid and CaR-transfected HEK293 cells. Am. J. Physiol. Renal Physiol. 280, F291–F302 (2001).
Mamillapalli, R., VanHouten, J., Zawalich, W. & Wysolmerski, J. Switching of G-protein usage by the calcium-sensing receptor reverses its effect on parathyroid hormone-related protein secretion in normal versus malignant breast cells. J. Biol. Chem. 283, 24435–24447 (2008).
Mamillapalli, R. & Wysolmerski, J. The calcium-sensing receptor couples to Gαs and regulates PTHrP and ACTH secretion in pituitary cells. J. Endocrinol. 204, 287–297 (2010).
Huang, C., Hujer, K. M., Wu, Z. & Miller, R. T. The Ca2+-sensing receptor couples to Gα12/13 to activate phospholipase D in Madin-Darby canine kidney cells. Am. J. Physiol. Cell Physiol. 286, C22–C30 (2004).
Abid, H. A., Inoue, A. & Gorvin, C. M. Heterogeneity of G protein activation by the calcium-sensing receptor. J. Mol. Endocrinol. 67, 41–53 (2021).
Liang, Y. L. et al. Dominant negative G proteins enhance formation and purification of agonist-GPCR-G protein complexes for structure determination. ACS Pharmacol. Transl. Sci. 1, 12–20 (2018).
Nehme, R. et al. Mini-G proteins: novel tools for studying GPCRs in their active conformation. PLoS ONE 12, e0175642 (2017).
Geng, Y. et al. Structural mechanism of ligand activation in human calcium-sensing receptor. eLife 5, e13662 (2016).
Zhang, C. et al. Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist. Sci. Adv. 2, e1600241 (2016).
Nemeth, E. F. Allosteric modulators of the extracellular calcium receptor. Drug Discov. Today Technol.10, e277–e284 (2013).
Rasmussen, S. G. et al. Crystal structure of the β2 adrenergic receptor–Gs protein complex. Nature 477, 549–555 (2011).
Maeda, S. et al. Development of an antibody fragment that stabilizes GPCR/G-protein complexes. Nat. Commun. 9, 3712 (2018).
Park, J. et al. Symmetric activation and modulation of the human calcium-sensing receptor. Proc. Natl Acad. Sci. USA 118, e2115849118 (2021).
Isberg, V. et al. Generic GPCR residue numbers—aligning topology maps while minding the gaps. Trends Pharmacol. Sci. 36, 22–31 (2015).
Ray, K., Fan, G. F., Goldsmith, P. K. & Spiegel, A. M. The carboxyl terminus of the human calcium receptor. Requirements for cell-surface expression and signal transduction. J. Biol. Chem. 272, 31355–31361 (1997).
Gama, L. & Breitwieser, G. E. A carboxyl-terminal domain controls the cooperativity for extracellular Ca2+ activation of the human calcium sensing receptor. A study with receptor-green fluorescent protein fusions. J. Biol. Chem. 273, 29712–29718 (1998).
Chang, W., Chen, T. H., Pratt, S. & Shoback, D. Amino acids in the second and third intracellular loops of the parathyroid Ca2+-sensing receptor mediate efficient coupling to phospholipase C. J. Biol. Chem. 275, 19955–19963 (2000).
Goolam, M. A. et al. Roles of intraloops-2 and -3 and the proximal C-terminus in signalling pathway selection from the human calcium-sensing receptor. FEBS Lett. 588, 3340–3346 (2014).
Gao, Y. et al. Asymmetric activation of the calcium-sensing receptor homodimer. Nature 595, 455–459 (2021).
Wen, T. et al. Structural basis for activation and allosteric modulation of full-length calcium-sensing receptor. Sci. Adv. 7, eabg1483 (2021).
Ling, S. et al. Structural mechanism of cooperative activation of the human calcium-sensing receptor by Ca2+ ions and L-tryptophan. Cell Res. 31, 383–394 (2021).
Chen, X. et al. Structural insights into the activation of human calcium-sensing receptor. eLife 10, e68578 (2021).
Wall, M. A. et al. The structure of the G protein heterotrimer Giα1β1γ2. Cell 83, 1047–1058 (1995).
Flock, T. et al. Universal allosteric mechanism for Gα activation by GPCRs. Nature 524, 173–179 (2015).
Conklin, B. R., Farfel, Z., Lustig, K. D., Julius, D. & Bourne, H. R. Substitution of three amino acids switches receptor specificity of Gqα to that of Giα. Nature 363, 274–276 (1993).
Conklin, B. R. et al. Carboxyl-terminal mutations of Gq alpha and Gs alpha that alter the fidelity of receptor activation. Mol. Pharmacol. 50, 885–890 (1996).
Bettler, B., Kaupmann, K., Mosbacher, J. & Gassmann, M. Molecular structure and physiological functions of GABAB receptors. Physiol. Rev. 84, 835–867 (2004).
Pollak, M. R. et al. Mutations in the human Ca2+-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism. Cell 75, 1297–1303 (1993).
Goehring, A. et al. Screening and large-scale expression of membrane proteins in mammalian cells for structural studies. Nat. Protoc. 9, 2574–2585 (2014).
Gorkhali, R. et al. Extracellular calcium alters calcium-sensing receptor network integrating intracellular calcium-signaling and related key pathway. Sci. Rep. 11, 20576 (2021).
Ritchie, T. K. et al. Chapter 11—Reconstitution of membrane proteins in phospholipid bilayer nanodiscs. Methods Enzymol. 464, 211–231 (2009).
Reeves, P. J., Callewaert, N., Contreras, R. & Khorana, H. G. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA 99, 13419–13424 (2002).
Bepler, T. et al. Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs. Nat. Methods 16, 1153–1160 (2019).
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213–221 (2010).
Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010).
Thom, C. et al. Structures of neurokinin 1 receptor in complex with Gq and Gs proteins reveal substance P binding mode and unique activation features. Sci. Adv. 7, eabk2872 (2021).
Qu, X. et al. Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1. Nature 604, 779–785 (2022).
Cao, C. et al. Structure, function and pharmacology of human itch GPCRs. Nature 600, 170–175 (2021).
Johnson, R. M. et al. Cryo-EM structure of the dual incretin receptor agonist, peptide-19, in complex with the glucagon-like peptide-1 receptor. Biochem. Biophys. Res. Commun. 578, 84–90 (2021).
Moriarty, N. W., Grosse-Kunstleve, R. W. & Adams, P. D. electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta Crystallogr. D Biol. Crystallogr. 65, 1074–1080 (2009).
Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12–21 (2010).
Novotny, M., Madsen, D. & Kleywegt, G. J. Evaluation of protein fold comparison servers. Proteins 54, 260–270 (2004).
Goddard, T. D. et al. UCSF ChimeraX: meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018).
Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013).
Schrage, R. et al. The experimental power of FR900359 to study Gq-regulated biological processes. Nat. Commun. 6, 10156 (2015).
Olsen, R. H. J. et al. TRUPATH, an open-source biosensor platform for interrogating the GPCR transducerome. Nat. Chem. Biol. 16, 841–849 (2020).
[ad_2]
Source link