Concomitant action of structural elements and receptor phosphorylation determines arrestin-3 interaction with the free fatty acid receptor FFA4

Journal of Biological Chemistry

Volumn 289, Issue 26, 2014, Pages 18451-18465

  Butcher, Adrian J ^a   Hudson, Brian D ^b   Shimpukade, Bharat ^c   Alvarez Curto, Elisa ^b   Prihandoko, Rudi ^a   Ulven, Trond ^c   Milligan, Graeme ^b   Tobin, Andrew B ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

^c UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

LIGANDS; MASS SPECTROMETRY; MUTAGENESIS; PHOSPHORYLATION;

DIFFERENTIAL COUPLING; G PROTEIN COUPLED RECEPTORS; INFLAMMATORY RESPONSE; LONG CHAIN FATTY ACID; PHOSPHORYLATION SITES; PHOSPHOSPECIFIC ANTIBODIES; STRUCTURAL COMPONENT; STRUCTURAL ELEMENTS;

FATTY ACIDS;

ARRESTIN 3; ASPARTIC ACID; FREE FATTY ACID RECEPTOR 4; GLUTAMIC ACID; PHOSPHOPEPTIDE; RECEPTOR; RETINA S ANTIGEN; SERINE; THREONINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIBODY SPECIFICITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; MASS SPECTROMETRY; MUTAGENESIS; NONHUMAN; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION;

ARRESTIN; DIABETES; FATTY ACID; G PROTEIN; G PROTEIN-COUPLED RECEPTOR (GPCR); PHOSPHORYLATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ARRESTINS; CELL LINE; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN BINDING; RECEPTORS, G-PROTEIN-COUPLED;

EID: 84903513580     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.568816     Document Type: Article

References (33)

1. Ryan, K. K., and Seeley, R. J. (2013) Physiology. Food as a hormone. Science 339, 918-919
2. Ichimura, A., Hirasawa, A., Hara, T., and Tsujimoto, G. (2009) Free fatty acid receptors act as nutrient sensors to regulate energy homeostasis. Prostaglandins Other Lipid Mediat. 89, 82-88
3. Stoddart, L. A., Smith, N. J., and Milligan, G. (2008) International Union of Pharmacology. LXXI. Free fatty acid receptors FFA1, -2, and -3: pharmacology and pathophysiological functions. Pharmacol. Rev. 60, 405-417
4. Mancini, A. D., and Poitout, V. (2013) The fatty acid receptor FFA1/GPR40 a decade later: how much do we know? Trends Endocrinol. Metab. 24, 398-407
5. Talukdar, S., Olefsky, J. M., and Osborn, O. (2011) Targeting GPR120 and other fatty acid-sensing GPCRs ameliorates insulin resistance and inflammatory diseases. Trends Pharmacol. Sci. 32, 543-550
6. Holliday, N. D., Watson, S. J., and Brown, A. J. (2011) Drug discovery opportunities and challenges at G protein coupled receptors for long chain free fatty acids. Front. Endocrinol. 2, 112
7. Hudson, B. D., Ulven, T., and Milligan, G. (2013) The therapeutic potential of allosteric ligands for free fatty acid sensitive GPCRs. Curr. Top. Med. Chem. 13, 14-25
8. Ulven, T. (2012) Short-chain free fatty acid receptors FFA2/GPR43 and FFA3/GPR41 as new potential therapeutic targets. Front. Endocrinol. 3, 111
9. Burant, C. F., Viswanathan, P., Marcinak, J., Cao, C., Vakilynejad, M., Xie, B., and Leifke, E. (2012) TAK-875 versus placebo or glimepiride in type 2 diabetes mellitus: a phase 2, randomised, double-blind, placebo-controlled trial. Lancet 379, 1403-1411
10. Kaku, K., Araki, T., and Yoshinaka, R. (2013) Randomized, double-blind, dose-ranging study of TAK-875, a novel GPR40 agonist, in Japanese patients with inadequately controlled type 2 diabetes. Diabetes Care 36, 245-250
11. Hirasawa, A., Tsumaya, K., Awaji, T., Katsuma, S., Adachi, T., Yamada, M., Sugimoto, Y., Miyazaki, S., and Tsujimoto, G. (2005) Free fatty acids regulate gut incretin glucagon-like peptide-1 secretion through GPR120. Nat. Med. 11, 90-94
12. Taneera, J., Lang, S., Sharma, A., Fadista, J., Zhou, Y., Ahlqvist, E., Jonsson, A., Lyssenko, V., Vikman, P., Hansson, O., Parikh, H., Korsgren, O., Soni, A., Krus, U., Zhang, E., Jing, X. J., Esguerra, J. L., Wollheim, C. B., Salehi, A., Rosengren, A., Renström, E., and Groop, L. (2012) A systems genetics approach identifies genes and pathways for type 2 diabetes in human islets. CellMetab. 16, 122-134
13. Oh, D. Y., Talukdar, S., Bae, E. J., Imamura, T., Morinaga, H., Fan, W., Li, P., Lu, W. J., Watkins, S. M., and Olefsky, J. M. (2010) GPR120 is an ω-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects. Cell 142, 687-698
14. Ichimura, A., Hirasawa, A., Poulain-Godefroy, O., Bonnefond, A., Hara, T., Yengo, L., Kimura, I., Leloire, A., Liu, N., Iida, K., Choquet, H., Besnard, P., Lecoeur, C., Vivequin, S., Ayukawa, K., Takeuchi, M., Ozawa, K., Tauber, M., Maffeis, C., Morandi, A., Buzzetti, R., Elliott, P., Pouta, A., Jarvelin, M. R., Körner, A., Kiess, W., Pigeyre, M., Caiazzo, R., Van Hul, W., Van Gaal, L., Horber, F., Balkau, B., Lévy-Marchal, C., Rouskas, K., Kouvatsi, A., Hebebrand, J., Hinney, A., Scherag, A., Pattou, F., Meyre, D., Koshimizu, T. A., Wolowczuk, I., Tsujimoto, G., and Froguel, P. (2012) Dysfunction of lipid sensor GPR120 leads to obesity in both mouse and human. Nature 483, 350-354
15. Shimpukade, B., Hudson, B. D., Hovgaard, C. K., Milligan, G., and Ulven, T. (2012) Discovery of a potent and selective GPR120 agonist. J. Med. Chem. 55, 4511-4515
16. Hudson, B. D., Shimpukade, B., Mackenzie, A. E., Butcher, A. J., Pediani, J. D., Christiansen, E., Heathcote, H., Tobin, A. B., Ulven, T., and Milligan, G. (2013) The pharmacology of a potent and selective agonist, TUG-891, demonstrates both potential opportunity and possible challenges to therapeutic agonism of FFA4 (GPR120). Mol. Pharmacol. 84, 710-725
17. Sänchez-Reyes, O. B., Romero-Ávila, M. T., Castillo-Badillo, J. A., Takei, Y., Hirasawa, A., Tsujimoto, G., Villalobos-Molina, R., and García-Säinz, J. A. (2014) Free fatty acids and protein kinase C activation induce GPR120 (free fatty acid receptor 4) phosphorylation. Eur. J. Pharmacol. 723, 368-374
18. Kenakin, T. (2009) Biased agonism. F1000 Biol. Rep. 1, 87
19. Hudson, B. D., Smith, N. J., and Milligan, G. (2011) Experimental challenges to targeting poorly characterized GPCRs: uncovering the therapeutic potential for free fatty acid receptors. Adv. Pharmacol. 62, 175-218
20. 357 in the C-terminal tail. Biochem. Pharmacol. 87, 650-659
21. Butcher, A. J., Prihandoko, R., Kong, K. C., McWilliams, P., Edwards, J. M., Bottrill, A., Mistry, S., and Tobin, A. B. (2011) Differential G-proteincoupled receptor phosphorylation provides evidence for a signaling bar code. J. Biol. Chem. 286, 11506-11518
22. 2-adrenergic receptor establish a barcode that encodes differential functions ofβ-arrestin. Sci. Signal. 4, ra51
23. Busillo, J. M., Armando, S., Sengupta, R., Meucci, O., Bouvier, M., and Benovic, J. L. (2010) Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling. J. Biol. Chem. 285, 7805-7817
24. Hinkle, P. M., Gehret, A. U., and Jones, B. W. (2012) Desensitization, trafficking, and resensitization of the pituitary thyrotropin-releasing hormone receptor. Front. Neurosci. 6, 180
25. Gehret, A. U., and Hinkle, P. M. (2010) Importance of regions outside the cytoplasmic tail of G-protein-coupled receptors for phosphorylation and dephosphorylation. Biochem. J. 428, 235-245
26. Ghosh, M., and Schonbrunn, A. (2011) Differential temporal and spatial regulation of somatostatin receptor phosphorylation and dephosphorylation. J. Biol. Chem. 286, 13561-13573
27. Tobin, A. B., Butcher, A. J., and Kong, K. C. (2008) Location, location, location. Site-specific GPCR phosphorylation offers a mechanism for celltype-specific signalling. Trends Pharmacol. Sci. 29, 413-420
28. Shukla, A. K., Manglik, A., Kruse, A. C, Xiao, K., Reis, R. I., Tseng, W. C, Staus, D. P., Hilger, D., Uysal, S., Huang, L. Y., Paduch, M., Tripathi-Shukla, P., Koide, A., Koide, S., Weis, W. I., Kossiakoff, A. A., Kobilka, B. K., and Lefkowitz, R. J. (2013) Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497, 137-141
29. Martini, L., Hastrup, H., Holst, B., Fraile-Ramos, A., Marsh, M., Schwartz, T. W. (2002) NK1 receptor fused to β-arrestin displays a single-component, high-affinity molecular phenotype. Mol. Pharmacol. 62, 30-37
30. Kenakin, T. (2005) New concepts in drug discovery: collateral efficacy and permissive antagonism. Nat Rev. Drug Discov. 4, 919-927
31. Rajagopal, S., Rajagopal, K., and Lefkowitz, R. J. (2010) Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 9, 373-386
32. Violin, J. D., and Lefkowitz, R. J. (2007) β-Arrestin-biased ligands at seventransmembrane receptors. Trends Pharmacol. Sci. 28, 416-422
33. Kenakin, T., and Christopoulos, A. (2013) Signalling bias in new drug discovery: detection, quantification and therapeutic impact. Nat. Rev. Drug Discov. 12, 205-216