Classification, nomenclature, and structural aspects of adhesion GPCRs

Handbook of Experimental Pharmacology

Volumn 234, Issue , 2016, Pages 15-41

  Krishnan, Arunkumar ^a   Nijmeijer, Saskia ^b   de Graaf, Chris ^b   Schiöth, Helgi B ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b AMSTERDAM INSTITUTE FOR MOLECULES   (Netherlands)

Author keywords

Adhesion GPCRs; Classification; Drug targets; GAIN domain; Homologs; Mammals; Model organisms; Nomenclature; Pharmacology; Vertebrates

Indexed keywords

ADGRA1 PROTEIN; ADGRA2 PROTEIN; ADGRA3 PROTEIN; ADGRB1 PROTEIN; ADGRB3 PROTEIN; ADGRC1 PROTEIN; ADGRC2 PROTEIN; ADGRC3 PROTEIN; ADGRD1 PROTEIN; ADGRD2 PROTEIN; ADGRE2 PROTEIN; ADGRE3 PROTEIN; ADGRE4 PROTEIN; ADGRE5 PROTEIN; ADGRF1 PROTEIN; ADGRF2 PROTEIN; ADGRF4 PROTEIN; ADGRG1 PROTEIN; ADGRG2 PROTEIN; ADGRG3 PROTEIN; ADGRG4 PROTEIN; ADGRG5 PROTEIN; ADGRL1 PROTEIN; ADGRL2 PROTEIN; ADGRL3 PROTEIN; ADGRV PROTEIN; G PROTEIN COUPLED RECEPTOR; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; COMPLEX FORMATION; HUMAN; INVERTEBRATE; MOLECULAR EVOLUTION; MOLECULAR PHYLOGENY; NOMENCLATURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; VERTEBRATE; ANIMAL; CELL ADHESION; CELL MEMBRANE; CHEMISTRY; CLASSIFICATION; GENETICS; METABOLISM; PHYLOGENY; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

ANIMALS; CELL ADHESION; CELL MEMBRANE; HUMANS; PHYLOGENY; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; TERMINOLOGY AS TOPIC;

EID: 84995460989     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-319-41523-9_2     Document Type: Chapter

References (131)

1. Fredriksson R, Lagerstrom MC, Lundin LG, Schioth HB (2003) The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63(6):1256-1272. doi:10.1124/mol.63.6.1256
2. Schioth HB, Fredriksson R (2005) The GRAFS classification system of G-protein coupled receptors in comparative perspective. Gen Comp Endocrinol 142(1-2):94-101. doi:10.1016/j.ygcen.2004.12.018
3. Baud V, Chissoe SL, Viegas-Pequignot E, Diriong S, N’Guyen VC, Roe BA et al (1995) EMR1, an unusual member in the family of hormone receptors with seven transmembrane segments. Genomics 26(2):334-344
4. Gray JX, Haino M, Roth MJ, Maguire JE, Jensen PN, Yarme A et al (1996) CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation. J Immunol 157(12):5438-5447
5. Hamann J, Eichler W, Hamann D, Kerstens HM, Poddighe PJ, Hoovers JM et al (1995) Expression cloning and chromosomal mapping of the leukocyte activation antigen CD97, a new seven-span transmembrane molecule of the secretion receptor superfamily with an unusual extracellular domain. J Immunol 155(4):1942-1950
6. Kwakkenbos MJ, Kop EN, Stacey M, Matmati M, Gordon S, Lin HH et al (2004) The EGF-TM7 family: a postgenomic view. Immunogenetics 55(10):655-666. doi:10.1007/s00251-003-0625-2
7. Zendman AJ, Cornelissen IM, Weidle UH, Ruiter DJ, van Muijen GN (1999) TM7XN1, a novel human EGF-TM7-like cDNA, detected with mRNA differential display using human melanoma cell lines with different metastatic potential. FEBS Lett 446(2-3):292-298
8. Stacey M, Lin HH, Gordon S, McKnight AJ (2000) LNB-TM7, a group of seventransmembrane proteins related to family-B G-protein-coupled receptors. Trends Biochem Sci 25(6):284-289
9. Harmar AJ (2001) Family-B G-protein-coupled receptors. Genome Biol 2(12): REVIEWS 3013. PubMed PMID: 11790261; PubMed Central PMCID: PMCPMC138994
10. Fredriksson R, Gloriam DE, Hoglund PJ, Lagerstrom MC, Schioth HB (2003) There exist at least 30 human G-protein-coupled receptors with long Ser/Thr-rich N-termini. Biochem Biophys Res Commun 301(3):725-734
11. Langenhan T, Aust G, Hamann J (2013) Sticky signaling-adhesion class G protein-coupled receptors take the stage. Sci Signal 6(276):re3. doi:10.1126/scisignal.2003825
12. Arac D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Sudhof TC et al (2012) A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis. EMBO J 31(6):1364-1378. doi:10.1038/emboj.2012.26, PubMed PMID: 22333914; PubMed Central PMCID: PMCPMC3321182
13. Lagerstrom MC, Schioth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7(4):339-357. doi:10.1038/nrd2518
14. Poyner DR, Hay DL (2012) Secretin family (Class B) G protein-coupled receptors-from molecular to clinical perspectives. Br J Pharmacol 166(1):1-3. doi:10.1111/j.1476-5381.2011.01810.x, PubMed PMID: 22489621; PubMed Central PMCID: PMCPMC3415632
15. Hamann J, Aust G, Arac D, Engel FB, Formstone C, Fredriksson R et al (2015) International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors. Pharmacol Rev 67(2):338-367. doi:10.1124/pr.114.009647, PubMed PMID: 25713288, PubMed Central PMCID: PMC4394687
16. Bjarnadottir TK, Fredriksson R, Hoglund PJ, Gloriam DE, Lagerstrom MC, Schioth HB (2004) The human and mouse repertoire of the adhesion family of G-protein-coupled receptors. Genomics 84(1):23-33. doi:10.1016/j.ygeno.2003.12.004
17. Yang Z, Rannala B (2012) Molecular phylogenetics: principles and practice. Nat Rev Genet 13(5):303-314. doi:10.1038/nrg3186
18. Gloriam DE, Fredriksson R, Schioth HB (2007) The G protein-coupled receptor subset of the rat genome. BMC Genomics 8:338. doi:10.1186/1471-2164-8-338, PubMed PMID: 17892602, PubMed Central PMCID: PMC2117022
19. Haitina T, Fredriksson R, Foord SM, Schioth HB, Gloriam DE (2009) The G protein-coupled receptor subset of the dog genome is more similar to that in humans than rodents. BMC Genomics 10:24. doi:10.1186/1471-2164-10-24, PubMed PMID: 19146662, PubMed Central PMCID: PMC2651185
20. Bjarnadottir TK, Gloriam DE, Hellstrand SH, Kristiansson H, Fredriksson R, Schioth HB (2006) Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse. Genomics 88(3):263-273. doi:10.1016/j.ygeno.2006.04.001
21. Haitina T, Olsson F, Stephansson O, Alsio J, Roman E, Ebendal T et al (2008) Expression profile of the entire family of Adhesion G protein-coupled receptors in mouse and rat. BMC Neurosci 9:43. doi:10.1186/1471-2202-9-43, PubMed PMID: 18445277, PubMed Central PMCID: PMC2386866
22. Lagerstrom MC, Hellstrom AR, Gloriam DE, Larsson TP, Schioth HB, Fredriksson R (2006) The G protein-coupled receptor subset of the chicken genome. PLoS Comput Biol 2(6), e54. doi:10.1371/journal.pcbi.0020054, PubMed PMID: 16741557, PubMed Central PMCID: PMC1472694
23. Metpally RP, Sowdhamini R (2005) Genome wide survey of G protein-coupled receptors in Tetraodon nigroviridis. BMC Evol Biol 5:41. doi:10.1186/1471-2148-5-41, PubMed PMID: 16022726, PubMed Central PMCID: PMC1187884
24. Harty BL, Krishnan A, Sanchez NE, Schioth HB, Monk KR (2015) Defining the gene repertoire and spatiotemporal expression profiles of adhesion G protein-coupled receptors in zebrafish. BMC Genomics 16:62. doi:10.1186/s12864-015-1296-8, PubMed PMID: 25715737, PubMed Central PMCID: PMC4335454
25. Kamesh N, Aradhyam GK, Manoj N (2008) The repertoire of G protein-coupled receptors in the sea squirt Ciona intestinalis. BMC Evol Biol 8:129. doi:10.1186/1471-2148-8-129, PubMed PMID: 18452600, PubMed Central PMCID: PMC2396169
26. Nordstrom KJ, Fredriksson R, Schioth HB (2008) The amphioxus (Branchiostoma floridae) genome contains a highly diversified set of G protein-coupled receptors. BMC Evol Biol 8:9. doi:10.1186/1471-2148-8-9, PubMed PMID: 18199322, PubMed Central PMCID: PMC2246102
27. Krishnan A, Almen MS, Fredriksson R, Schioth HB (2013) Remarkable similarities between the hemichordate (Saccoglossus kowalevskii) and vertebrate GPCR repertoire. Gene 526 (2):122-133. doi:10.1016/j.gene.2013.05.005
28. Raible F, Tessmar-Raible K, Arboleda E, Kaller T, Bork P, Arendt D et al (2006) Opsins and clusters of sensory G-protein-coupled receptors in the sea urchin genome. Dev Biol 300 (1):461-475. doi:10.1016/j.ydbio.2006.08.070
29. Yona S, Lin HH, Siu WO, Gordon S, Stacey M (2008) Adhesion-GPCRs: emerging roles for novel receptors. Trends Biochem Sci 33(10):491-500. doi:10.1016/j.tibs.2008.07.005
30. Nagarathnam B, Kalaimathy S, Balakrishnan V, Sowdhamini R (2012) Cross-genome clustering of human and C elegans G-protein coupled receptors. Evol Bioinform Online 8:229-259. doi:10.4137/EBO.S9405, PubMed PMID: 22807621, PubMed Central PMCID: PMC3396462
31. Metpally RP, Sowdhamini R (2005) Cross genome phylogenetic analysis of human and Drosophila G protein-coupled receptors: application to functional annotation of orphan receptors. BMC Genomics 6:106. doi:10.1186/1471-2164-6-106, PubMed PMID: 16091152, PubMed Central PMCID: PMC1192796
32. Nordstrom KJ, Lagerstrom MC, Waller LM, Fredriksson R, Schioth HB (2009) The Secretin GPCRs descended from the family of Adhesion GPCRs. Mol Biol Evol 26(1):71-84. doi:10.1093/molbev/msn228
33. Nordstrom KJ, Sallman Almen M, Edstam MM, Fredriksson R, Schioth HB (2011) Independent HHsearch, Needleman-Wunsch-based, and motif analyses reveal the overall hierarchy for most of the G protein-coupled receptor families. Mol Biol Evol 28(9):2471-2480. doi:10.1093/molbev/msr061
34. Krishnan A, Dnyansagar R, Almen MS, Williams MJ, Fredriksson R, Manoj N et al (2014) The GPCR repertoire in the demosponge Amphimedon queenslandica: insights into the GPCR system at the early divergence of animals. BMC Evol Biol 14:270. doi:10.1186/s12862-014-0270-4, PubMed PMID: 25528161, PubMed Central PMCID: PMC4302439
35. Krishnan A, Schioth HB (2015) The role of G protein-coupled receptors in the early evolution of neurotransmission and the nervous system. J Exp Biol 218(Pt 4):562-571. doi:10.1242/jeb.110312
36. Bjarnadottir TK, Fredriksson R, Schioth HB (2007) The adhesion GPCRs: a unique family of G protein-coupled receptors with important roles in both central and peripheral tissues. Cell Mol Life Sci 64(16):2104-2119. doi:10.1007/s00018-007-7067-1
37. Liebscher I, Schon J, Petersen SC, Fischer L, Auerbach N, Demberg LM et al (2014) A tethered agonist within the ectodomain activates the adhesion G protein-coupled receptors GPR126 and GPR 133. Cell Rep 9(6):2018-2026. doi:10.1016/j.celrep.2014.11.036, PubMed PMID: 25533341, PubMed Central PMCID: PMC4277498
38. Stoveken HM, Hajduczok AG, Xu L, Tall GG (2015) Adhesion G protein-coupled receptors are activated by exposure of a cryptic tethered agonist. Proc Natl Acad Sci U S A 112 (19):6194-6199. doi:10.1073/pnas.1421785112, PubMed PMID: 25918380, PubMed Central PMCID: PMC4434738
39. Demberg LM, Rothemund S, Schoneberg T, Liebscher I (2015) Identification of the tethered peptide agonist of the adhesion G protein-coupled receptor GPR64/ADGRG 2. Biochem Biophys Res Commun 464(3):743-747. doi:10.1016/j.bbrc.2015.07.020
40. Wilde C, Fischer L, Lede V, Kirchberger J, Rothemund S, Schoneberg T et al (2016) The constitutive activity of the adhesion GPCR GPR114/ADGRG5 is mediated by its tethered agonist. FASEB J 30(2):666-673. doi:10.1096/fj.15-276220
41. Liebscher I, Schöneberg T (2016) Tethered agonism: a common activation mechanism of adhesion GPCRs. In: Langenhan T, Schöneberg T (eds) Adhesion G protein-coupled receptors: molecular, physiological and pharmacological principles in health and disease. Springer, Heidelberg
42. Arac¸ D, Sträter N, Seiradake E (2016) Understanding the structural basis of adhesion GPCR functions. In: Langenhan T, Schöneberg T (eds) Adhesion G protein-coupled receptors: molecular, physiological and pharmacological principles in health and disease. Springer, Heidelberg
43. Lin HH, Stacey M, Yona S, Chang GW (2010) GPS proteolytic cleavage of adhesion-GPCRs. Adv Exp Med Biol 706:49-58, PMID: 21618825
44. Promel S, Langenhan T, Arac D (2013) Matching structure with function: the GAIN domain of adhesion-GPCR and PKD1-like proteins. Trends Pharmacol Sci 34(8):470-478. doi:10.1016/j.tips.2013.06.002
45. Promel S, Frickenhaus M, Hughes S, Mestek L, Staunton D, Woollard A et al (2012) The GPS motif is a molecular switch for bimodal activities of adhesion class G protein-coupled receptors. Cell Rep 2(2):321-331. doi:10.1016/j.celrep.2012.06.015, PubMed PMID: 22938866, PubMed Central PMCID: PMC3776922
46. Formstone CJ, Moxon C, Murdoch J, Little P, Mason I (2010) Basal enrichment within neuroepithelia suggests novel function(s) for Celsr1 protein. Mol Cell Neurosci 44 (3):210-222. doi:10.1016/j.mcn.2010.03.008
47. Nieberler M, Kittel RJ, Petrenko AG, Lin H-H, Langenhan T (2016) Control of adhesion GPCR function through proteolytic processing. In: Langenhan T, Schöneberg T (eds) Adhesion G protein-coupled receptors: molecular, physiological and pharmacological principles in health and disease. Springer, Heidelberg
48. Paavola KJ, Hall RA (2012) Adhesion G protein-coupled receptors: signaling, pharmacology, and mechanisms of activation. Mol Pharmacol 82(5):777-783. doi:10.1124/mol.112.080309, PubMed PMID: 22821233, PubMed Central PMCID: PMC3477231
49. Underwood CR, Garibay P, Knudsen LB, Hastrup S, Peters GH, Rudolph R et al (2010) Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor. J Biol Chem 285(1):723-730. doi:10.1074/jbc.M109.033829, PubMed PMID: 19861722, PubMed Central PMCID: PMC2804221
50. Wouters MA, Rigoutsos I, Chu CK, Feng LL, Sparrow DB, Dunwoodie SL (2005) Evolution of distinct EGF domains with specific functions. Protein Sci 14(4):1091-1103. doi:10.1110/ps.041207005, PubMed PMID: 15772310, PubMed Central PMCID: PMC2253431
51. Krasnoperov VG, Bittner MA, Beavis R, Kuang Y, Salnikow KV, Chepurny OG et al (1997) alpha-Latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor. Neuron 18(6):925-937
52. Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF et al (1997) Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G proteincoupled receptors. J Biol Chem 272(34):21504-21508
53. Tomarev SI, Nakaya N (2009) Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Mol Neurobiol 40(2):122-138. doi:10.1007/s12035-009-8076-x, PubMed PMID: 19554483, PubMed Central PMCID: PMC2936706
54. Matsushita H, Lelianova VG, Ushkaryov YA (1999) The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS Lett 443(3):348-352
55. Vakonakis I, Langenhan T, Promel S, Russ A, Campbell ID (2008) Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain. Structure 16(6):944-953. doi:10.1016/j.str.2008.02.020, PubMed PMID: 18547526, PubMed Central PMCID: PMC2430599
56. Terada T, Watanabe Y, Tateno H, Naganuma T, Ogawa T, Muramoto K et al (2007) Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs. Biochim Biophys Acta 1770(4):617-629. doi:10.1016/j.bbagen.2006.11.003
57. Silva JP, Lelianova V, Hopkins C, Volynski KE, Ushkaryov Y (2009) Functional crossinteraction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors. J Biol Chem 284(10):6495-6506. doi:10.1074/jbc.M806979200, PubMed PMID: 19124473, PubMed Central PMCID: PMC2649109
58. Jackson VA, del Toro D, Carrasquero M, Roversi P, Harlos K, Klein R et al (2015) Structural basis of latrophilin-FLRT interaction. Structure 23(4):774-781. doi:10.1016/j.str.2015.01.013, PubMed PMID: 25728924, PubMed Central PMCID: PMC4396693
59. Silva JP, Ushkaryov YA (2010) The latrophilins, “split-personality” receptors. Adv Exp Med Biol 706:59-75, PubMed PMID: 21618826, PubMed Central PMCID: PMC3145135
60. Favara DM, Banham AH, Harris AL (2014) A review of ELTD1, a pro-angiogenic adhesion GPCR. Biochem Soc Trans 42(6):1658-1664. doi:10.1042/BST20140216
61. Nechiporuk T, Urness LD, Keating MT (2001) ETL, a novel seven-transmembrane receptor that is developmentally regulated in the heart. ETL is a member of the secretin family and belongs to the epidermal growth factor-seven-transmembrane subfamily. J Biol Chem 276 (6):4150-4157. doi:10.1074/jbc.M004814200
62. Rohou A, Nield J, Ushkaryov YA (2007) Insecticidal toxins from black widow spider venom. Toxicon 49(4):531-549. doi:10.1016/j.toxicon.2006.11.021, PubMed PMID: 17210168, PubMed Central PMCID: PMC2517654
63. Krasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG (1999) Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants. J Biol Chem 274(6):3590-3596
64. Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O et al (2011) Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A 108 (29):12113-12118. doi:10.1073/pnas.1019434108, PubMed PMID: 21724987, PubMed Central PMCID: PMC3141932
65. O’Sullivan ML, de Wit J, Savas JN, Comoletti D, Otto-Hitt S, Yates JR 3rd et al (2012) FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development. Neuron 73(5):903-910. doi:10.1016/j.neuron.2012.01.018, PubMed PMID: 22405201, PubMed Central PMCID: PMC3326387
66. Boucard AA, Maxeiner S, Sudhof TC (2014) Latrophilins function as heterophilic celladhesion molecules by binding to teneurins: regulation by alternative splicing. J Biol Chem 289(1):387-402. doi:10.1074/jbc.M113.504779, PubMed PMID: 24273166, PubMed Central PMCID: PMC3879561
67. Woelfle R, D’Aquila AL, Pavlovic T, Husic M, Lovejoy DA (2015) Ancient interaction between the teneurin C-terminal associated peptides (TCAP) and latrophilin ligand-receptor coupling: a role in behavior. Front Neurosci 9:146. doi:10.3389/fnins.2015.00146, PubMed PMID: 25964737, PubMed Central PMCID: PMC4408839
68. Lu YC, Nazarko OV, Sando R III, Salzman GS, Sudhof TC, Arac D (2015) Structural basis of latrophilin-FLRT-UNC5 interaction in cell adhesion. Structure 23(9):1678-1691. doi:10.1016/j.str.2015.06.024
69. Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S et al (2015) Structural and mechanistic insights into the latrophilin3-FLRT3 complex that mediates glutamatergic synapse development. Structure 23(9):1665-1677. doi:10.1016/j.str.2015.06.022
70. Petrenko AG, Surkova IN, Shamotienko OG, Kovalenko VA, Krasnoperov VN, Tret’iakov LA et al (1990) Study of the receptor for black widow spider neurotoxin. II. Isolation and characteristics of the receptor from bovine brain membranes. Bioorg Khim 16(2):158-165
71. Geppert M, Khvotchev M, Krasnoperov V, Goda Y, Missler M, Hammer RE et al (1998) Neurexin I alpha is a major alpha-latrotoxin receptor that cooperates in alpha-latrotoxin action. J Biol Chem 273(3):1705-1710
72. Hamann J, Kwakkenbos MJ, de Jong EC, Heus H, Olsen AS, van Lier RA (2003) Inactivation of the EGF-TM7 receptor EMR4 after the Pan-Homo divergence. Eur J Immunol 33 (5):1365-1371. doi:10.1002/eji.200323881
73. Kwakkenbos MJ, Matmati M, Madsen O, Pouwels W, Wang Y, Bontrop RE et al (2006) An unusual mode of concerted evolution of the EGF-TM7 receptor chimera EMR 2. FASEB J 20 (14):2582-2584. doi:10.1096/fj.06-6500fje
74. Lin HH, Stacey M, Hamann J, Gordon S, McKnight AJ (2000) Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD 97. Genomics 67 (2):188-200. doi:10.1006/geno.2000.6238
75. Hamann J, Vogel B, van Schijndel GM, van Lier RA (1996) The seven-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF). J Exp Med 184(3):1185-1189, PubMed PMID: 9064337, PubMed Central PMCID: PMC2192782
76. Hamann J, Stortelers C, Kiss-Toth E, Vogel B, Eichler W, van Lier RA (1998) Characterization of the CD55 (DAF)-binding site on the seven-span transmembrane receptor CD 97. Eur J Immunol 28(5):1701-1707. doi:10.1002/(SICI)1521-4141(199805)28:05<1701::AIDIMMU1701>3.0.CO;2-2
77. Lin HH, Stacey M, Saxby C, Knott V, Chaudhry Y, Evans D et al (2001) Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex. J Biol Chem 276(26):24160-24169. doi:10.1074/jbc.M101770200
78. Stacey M, Chang GW, Davies JQ, Kwakkenbos MJ, Sanderson RD, Hamann J et al (2003) The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood 102(8):2916-2924. doi:10.1182/blood-2002-11-3540
79. Wang T, Ward Y, Tian L, Lake R, Guedez L, Stetler-Stevenson WG et al (2005) CD97, an adhesion receptor on inflammatory cells, stimulates angiogenesis through binding integrin counter receptors on endothelial cells. Blood 105(7):2836-2844. doi:10.1182/blood-2004-07-2878
80. Wandel E, Saalbach A, Sittig D, Gebhardt C, Aust G (2012) Thy-1 (CD90) is an interacting partner for CD97 on activated endothelial cells. J Immunol 188(3):1442-1450. doi:10.4049/jimmunol.1003944
81. Kwakkenbos MJ, Pouwels W, Matmati M, Stacey M, Lin HH, Gordon S et al (2005) Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells. J Leukoc Biol 77(1):112-119. doi:10.1189/jlb.0704402
82. Ward Y, Lake R, Yin JJ, Heger CD, Raffeld M, Goldsmith PK et al (2011) LPA receptor heterodimerizes with CD97 to amplify LPA-initiated RHO-dependent signaling and invasion in prostate cancer cells. Cancer Res 71(23):7301-7311. doi:10.1158/0008-5472.CAN-11-2381
83. Ward Y, Lake R, Martin PL, Killian K, Salerno P, Wang T et al (2013) CD97 amplifies LPA receptor signaling and promotes thyroid cancer progression in a mouse model. Oncogene 32 (22):2726-2738. doi:10.1038/onc.2012.301
84. Veninga H, de Groot DM, McCloskey N, Owens BM, Dessing MC, Verbeek JS et al (2011) CD97 antibody depletes granulocytes in mice under conditions of acute inflammation via a Fc receptor-dependent mechanism. J Leukoc Biol 89(3):413-421. doi:10.1189/jlb.0510280
85. Fredriksson R, Lagerstrom MC, Hoglund PJ, Schioth HB (2002) Novel human G proteincoupled receptors with long N-terminals containing GPS domains and Ser/Thr-rich regions. FEBS Lett 531(3):407-414
86. Vallon M, Essler M (2006) Proteolytically processed soluble tumor endothelial marker (TEM) 5 mediates endothelial cell survival during angiogenesis by linking integrin alpha (v)beta3 to glycosaminoglycans. J Biol Chem 281(45):34179-34188. doi:10.1074/jbc.M605291200
87. Enkhbayar P, Kamiya M, Osaki M, Matsumoto T, Matsushima N (2004) Structural principles of leucine-rich repeat (LRR) proteins. Proteins 54(3):394-403. doi:10.1002/prot.10605
88. Vallon M, Aubele P, Janssen KP, Essler M (2012) Thrombin-induced shedding of tumour endothelial marker 5 and exposure of its RGD motif are regulated by cell-surface protein disulfide-isomerase. Biochem J 441(3):937-944. doi:10.1042/BJ20111682
89. Wang XJ, Zhang DL, Xu ZG, Ma ML, Wang WB, Li LL et al (2014) Understanding cadherin EGF LAG seven-pass G-type receptors. J Neurochem 131(6):699-711. doi:10.1111/jnc.12955, PubMed PMID: 25280249, PubMed Central PMCID: PMC4261025
90. Shapiro L, Weis WI (2009) Structure and biochemistry of cadherins and catenins. Cold Spring Harb Perspect Biol 1(3):a003053. doi:10.1101/cshperspect.a003053, PubMed PMID: 20066110, PubMed Central PMCID: PMC2773639
91. Overduin M, Harvey TS, Bagby S, Tong KI, Yau P, Takeichi M et al (1995) Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science 267(5196):386-389
92. Overduin M, Tong KI, Kay CM, Ikura M(1996) 1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin. J Biomol NMR 7(3):173-189
93. Takeichi M (1995) Morphogenetic roles of classic cadherins. Curr Opin Cell Biol 7 (5):619-627
94. Hohenester E, Tisi D, Talts JF, Timpl R (1999) The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell 4(5):783-792
95. Shima Y, Kawaguchi SY, Kosaka K, Nakayama M, Hoshino M, Nabeshima Y et al (2007) Opposing roles in neurite growth control by two seven-pass transmembrane cadherins. Nat Neurosci 10(8):963-969. doi:10.1038/nn1933
96. Zhang Y, Sivasankar S, Nelson WJ, Chu S (2009) Resolving cadherin interactions and binding cooperativity at the single-molecule level. Proc Natl Acad Sci U S A 106 (1):109-114. doi:10.1073/pnas.0811350106, PubMed PMID: 19114658, PubMed Central PMCID: PMC2629205
97. Goodman AR, Cardozo T, Abagyan R, Altmeyer A, Wisniewski HG, Vilcek J (1996) Long pentraxins: an emerging group of proteins with diverse functions. Cytokine Growth Factor Rev 7(2):191-202
98. Lum AM, Wang BB, Beck-Engeser GB, Li L, Channa N, Wabl M (2010) Orphan receptor GPR110, an oncogene overexpressed in lung and prostate cancer. BMC Cancer 10:40. doi:10.1186/1471-2407-10-40, PubMed PMID: 20149256, PubMed Central PMCID: PMC2830182
99. Bork P, Patthy L (1995) The SEA module: a new extracellular domain associated with O-glycosylation. Protein Sci 4(7):1421-1425. doi:10.1002/pro.5560040716, PubMed PMID: 7670383, PubMed Central PMCID: PMC2143162
100. LopezJimenez ND, Sainz E, Cavenagh MM, Cruz-Ithier MA, Blackwood CA, Battey JF et al (2005) Two novel genes, Gpr113, which encodes a family 2 G-protein-coupled receptor, and Trcg1, are selectively expressed in taste receptor cells. Genomics 85(4):472-482. doi:10.1016/j.ygeno.2004.12.005
101. Abe J, Suzuki H, Notoya M, Yamamoto T, Hirose S (1999) Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs. J Biol Chem 274(28):19957-19964
102. Abe J, Fukuzawa T, Hirose S (2002) Cleavage of Ig-Hepta at a “SEA” module and at a conserved G protein-coupled receptor proteolytic site. J Biol Chem 277(26):23391-23398. doi:10.1074/jbc.M110877200
103. Davies JQ, Chang GW, Yona S, Gordon S, Stacey M, Lin HH (2007) The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G proteincoupled receptors. J Biol Chem 282(37):27343-27353. doi:10.1074/jbc.M704096200
104. Fukuzawa T, Ishida J, Kato A, Ichinose T, Ariestanti DM, Takahashi T et al (2013) Lung surfactant levels are regulated by Ig-Hepta/GPR116 by monitoring surfactant protein D. PLoS One 8(7), e69451. doi:10.1371/journal.pone.0069451, PubMed PMID: 23922714, PubMed Central PMCID: PMC3726689
105. Koh JT, Kook H, Kee HJ, Seo YW, Jeong BC, Lee JH et al (2004) Extracellular fragment of brain-specific angiogenesis inhibitor 1 suppresses endothelial cell proliferation by blocking alphavbeta5 integrin. Exp Cell Res 294(1):172-184. doi:10.1016/j.yexcr.2003.11.008
106. Duman JG, Tu Y-K, Tolias KF (2016) Emerging roles of BAI adhesion-GPCRs in synapse development and plasticity. Neural Plast 2016:8301737. doi:10.1155/2016/8301737
107. Blanc G, Font B, Eichenberger D, Moreau C, Ricard-Blum S, Hulmes DJ et al (2007) Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity. J Biol Chem 282(23):16924-16933. doi:10.1074/jbc.M701610200
108. Tan K, Duquette M, Liu JH, Dong Y, Zhang R, Joachimiak A et al (2002) Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication. J Cell Biol 159 (2):373-382. doi:10.1083/jcb.200206062, PubMed PMID: 12391027, PubMed Central PMCID: PMC2173040
109. Das S, Owen KA, Ly KT, Park D, Black SG, Wilson JM et al (2011) Brain angiogenesis inhibitor 1 (BAI1) is a pattern recognition receptor that mediates macrophage binding and engulfment of Gram-negative bacteria. Proc Natl Acad Sci U S A 108(5):2136-2141. doi:10.1073/pnas.1014775108, PubMed PMID: 21245295, PubMed Central PMCID: PMC3033312
110. Kaur B, Brat DJ, Devi NS, Van Meir EG (2005) Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor 1, is an antiangiogenic and antitumorigenic factor. Oncogene 24 (22):3632-3642. doi:10.1038/sj.onc.1208317
111. Cork SM, Kaur B, Devi NS, Cooper L, Saltz JH, Sandberg EM et al (2012) A proprotein convertase/MMP-14 proteolytic cascade releases a novel 40 kDa vasculostatin from tumor suppressor BAI 1. Oncogene 31(50):5144-5152. doi:10.1038/onc.2012.1, PubMed PMID: 22330140, PubMed Central PMCID: PMC3355202
112. Park D, Tosello-Trampont AC, Elliott MR, Lu M, Haney LB, Ma Z et al (2007) BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module. Nature 450(7168):430-434. doi:10.1038/nature06329
113. Mazaheri F, Breus O, Durdu S, Haas P, Wittbrodt J, Gilmour D et al (2014) Distinct roles for BAI1 and TIM-4 in the engulfment of dying neurons by microglia. Nat Commun 5:4046. doi:10.1038/ncomms5046
114. Okajima D, Kudo G, Yokota H (2010) Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by proteolytic processing. J Recept Signal Transduct Res 30(3):143-153. doi:10.3109/10799891003671139
115. D’Souza SE, Ginsberg MH, Plow EF (1991) Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends Biochem Sci 16(7):246-250
116. Klenotic PA, Huang P, Palomo J, Kaur B, Van Meir EG, Vogelbaum MA et al (2010) Histidine-rich glycoprotein modulates the anti-angiogenic effects of vasculostatin. Am J Pathol 176(4):2039-2050. doi:10.2353/ajpath.2010.090782, PubMed PMID: 20167858, PubMed Central PMCID: PMC2843491
117. Bolliger MF, Martinelli DC, Sudhof TC (2011) The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins. Proc Natl Acad Sci U S A 108 (6):2534-2539. doi:10.1073/pnas.1019577108, PubMed PMID: 21262840, PubMed Central PMCID: PMC3038708
118. Moriguchi T, Haraguchi K, Ueda N, Okada M, Furuya T, Akiyama T (2004) DREG, a developmentally regulated G protein-coupled receptor containing two conserved proteolytic cleavage sites. Genes Cells 9(6):549-560. doi:10.1111/j.1356-9597.2004.00743.x
119. Wilde C, Fischer L, Lede V, Kirchberger J, Rothemund S, Schoneberg T et al (2015) The constitutive activity of the adhesion GPCR GPR114/ADGRG5 is mediated by its tethered agonist. FASEB J. doi:10.1096/fj.15-276220
120. Peeters MC, Fokkelman M, Boogaard B, Egerod KL, van de Water B, IJzerman AP et al (2015) The adhesion G protein-coupled receptor G2 (ADGRG2/GPR64) constitutively activates SRE and NFkappaB and is involved in cell adhesion and migration. Cell Signal 27 (12):2579-2588. doi:10.1016/j.cellsig.2015.08.015
121. Xu L, Begum S, Hearn JD, Hynes RO (2006) GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis. Proc Natl Acad Sci U S A 103(24):9023-9028. doi:10.1073/pnas.0602681103, PubMed PMID: 16757564, PubMed Central PMCID: PMC1474142
122. Luo R, Jeong SJ, Jin Z, Strokes N, Li S, Piao X (2011) G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination. Proc Natl Acad Sci U S A 108(31):12925-12930. doi:10.1073/pnas.1104821108, PubMed PMID: 21768377, PubMed Central PMCID: PMC3150909
123. Luo R, Jin Z, Deng Y, Strokes N, Piao X (2012) Disease-associated mutations prevent GPR56-collagen III interaction. PLoS One 7(1), e29818. doi:10.1371/journal.pone.0029818, PubMed PMID: 22238662, PubMed Central PMCID: PMC3251603
124. Yang L, Chen G, Mohanty S, Scott G, Fazal F, Rahman A et al (2011) GPR56 regulates VEGF production and angiogenesis during melanoma progression. Cancer Res 71 (16):5558-5568. doi:10.1158/0008-5472.CAN-10-4543, PubMed PMID: 21724588, PubMed Central PMCID: PMC3156271
125. Gupte J, Swaminath G, Danao J, Tian H, Li Y, Wu X (2012) Signaling property study of adhesion G-protein-coupled receptors. FEBS Lett 586(8):1214-1219. doi:10.1016/j.febslet.2012.03.014
126. Paavola KJ, Sidik H, Zuchero JB, Eckart M, Talbot WS (2014) Type IV collagen is an activating ligand for the adhesion G protein-coupled receptor GPR 126. Sci Signal 7(338): ra76. doi:10.1126/scisignal.2005347, PubMed PMID: 25118328; PubMed Central PMCID: PMC4159047
127. Petersen SC, Luo R, Liebscher I, Giera S, Jeong SJ, Mogha A et al (2015) The adhesion GPCR GPR126 has distinct, domain-dependent functions in Schwann cell development mediated by interaction with laminin-211. Neuron 85(4):755-769. doi:10.1016/j.neuron.2014.12.057, PubMed PMID: 25695270, PubMed Central PMCID: PMC4335265
128. McMillan DR, White PC (2010) Studies on the very large G protein-coupled receptor: from initial discovery to determining its role in sensorineural deafness in higher animals. Adv Exp Med Biol 706:76-86
129. Sun JP, Li R, Ren HZ, Xu AT, Yu X, Xu ZG (2013) The very large G protein coupled receptor (Vlgr1) in hair cells. J Mol Neurosci 50(1):204-214. doi:10.1007/s12031-012-9911-5
130. Nikkila H, McMillan DR, Nunez BS, Pascoe L, Curnow KM, White PC (2000) Sequence similarities between a novel putative G protein-coupled receptor and Na+/Ca2+ exchangers define a cation binding domain. Mol Endocrinol 14(9):1351-1364. doi:10.1210/mend.14.9.0511
131. McGee J, Goodyear RJ, McMillan DR, Stauffer EA, Holt JR, Locke KG et al (2006) The very large G-protein-coupled receptor VLGR1: a component of the ankle link complex required for the normal development of auditory hair bundles. J Neurosci 26(24):6543-6553. doi:10.1523/JNEUROSCI.0693-06.2006, PubMed PMID: 16775142, PubMed Central PMCID: PMC2682555