Functional consequences of naturally occurring DRY motif variants in the mammalian chemoattractant receptor GPR33

Genomics

Volumn 87, Issue 6, 2006, Pages 724-732

  Römpler, Holger ^a   Yu, Hon Tsen ^b   Arnold, Antje ^a   Orth, Annie ^c   Schöneberg, Torsten ^a  

^a Medical Faculty   (Germany)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^c UNIV MONTPELLIER   (France)

Author keywords

Chemokine; Constitutive activity; DRY motif; Evolution; G protein coupled receptor; Pseudogene

Indexed keywords

ARGININE; ASPARGYLARGINYLTYROSINE; CHEMOATTRACTANT; G PROTEIN COUPLED RECEPTOR; GLYCINE; HISTIDINE; PROTEIN GPR33; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

ALLELE; ARTICLE; CONTROLLED STUDY; FUNCTION TEST; GENE FUNCTION; GENE MUTATION; GENE SEQUENCE; GENETIC POLYMORPHISM; GENETIC VARIABILITY; HAMSTER; IN VITRO STUDY; MAMMAL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN MOTIF; PSEUDOGENE; SEQUENCE ANALYSIS; WILD TYPE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ANIMALS, WILD; CELL LINE; CERCOPITHECUS AETHIOPS; COS CELLS; CRICETINAE; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PSEUDOGENES; RECEPTORS, G-PROTEIN-COUPLED; SEQUENCE HOMOLOGY, AMINO ACID; VARIATION (GENETICS);

CRICETINAE; MAMMALIA; MUS MUSCULUS;

EID: 33646936560     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2006.02.009     Document Type: Article

References (33)

1. Ballesteros J.A., and Weinstein H. Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G-protein coupled receptors. Methods Neurosci. 25 (1995) 366-428
2. Wess J. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11 (1997) 346-354
3. Palczewski K., Kumasaka T., Hori T., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289 (2000) 739-745
4. Li J., Edwards P.C., Burghammer M., Villa C., and Schertler G.F. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343 (2004) 1409-1438
5. Alewijnse A.E., Timmerman H., Jacobs E.H., Smit M.J., Roovers E., Cotecchia S., and Leurs R. The effect of mutations in the DRY motif on the constitutive activity and structural instability of the histamine H2 receptor. Mol. Pharmacol. 57 (2000) 890-898
6. Rasmussen S.G., Jensen A.D., Liapakis G., Ghanouni P., Javitch J.A., and Gether U. Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56 (1999) 175-184
7. Franke R.R., Sakmar T.P., Graham R.M., and Khorana H.G. Structure and function in rhodopsin: studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267 (1992) 14767-14774
8. Jones P.G., Curtis C.A.M., and Hulme E.C. The function of a highly-conserved arginine residue in activation of the muscarinic M1 receptor. Eur. J. Pharmacol. 288 (1995) 251-257
9. Scheer A., Fanelli F., Costa T., De Benedetti P.G., and Cotecchia S. Constitutively active mutants of the a1B-adrenergic receptor: role of highly conserved polar amino acids in receptor activation. EMBO J. 15 (1996) 3566-3578
10. Zhu S.Z., Wang S.Z., Hu J., and el-Fakahany E.E. An arginine residue conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor. Mol. Pharmacol. 45 (1994) 517-523
11. Schöneberg T., Schulz A., Biebermann H., Hermsdorf T., Römpler H., and Sangkuhl K. Mutant G-protein-coupled receptors as a cause of human diseases. Pharmacol. Ther. 104 (2004) 173-206
12. Gaillard I., Rouquier S., Chavanieu A., Mollard P., and Giorgi D. Amino-acid changes acquired during evolution by olfactory receptor 912-93 modify the specificity of odorant recognition. Hum. Mol. Genet. 13 (2004) 771-780
13. Menashe I., Man O., Lancet D., and Gilad Y. Population differences in haplotype structure within a human olfactory receptor gene cluster. Hum. Mol. Genet. 11 (2002) 1381-1390
14. Zhang Z., Carriero N., and Gerstein M. Comparative analysis of processed pseudogenes in the mouse and human genomes. Trends Genet. 20 (2004) 62-67
15. Zhang Z., and Gerstein M. Large-scale analysis of pseudogenes in the human genome. Curr. Opin. Genet. Dev. 14 (2004) 328-335
16. Römpler H., Schulz A., Pitra C., Coop G., Przeworski M., Pääbo S., and Schöneberg T. The rise and fall of the chemoattractant receptor GPR33. J. Biol. Chem. 280 (2005) 31068-31075
17. Schöneberg T., Schulz A., Biebermann H., Grüters A., Grimm T., Hübschmann K., Filler G., Gudermann T., and Schultz G. V2 vasopressin receptor dysfunction in nephrogenic diabetes insipidus caused by different molecular mechanisms. Hum. Mutat. 12 (1998) 196-205
18. Schiöth H.B., Phillips S.R., Rudzish R., Birch-Machin M.A., Wikberg J.E., and Rees J.L. Loss of function mutations of the human melanocortin 1 receptor are common and are associated with red hair. Biochem. Biophys. Res. Commun. 260 (1999) 488-491
19. Chen A., Gao Z.G., Barak D., Liang B.T., and Jacobson K.A. Constitutive activation of A(3) adenosine receptors by site-directed mutagenesis. Biochem. Biophys. Res. Commun. 284 (2001) 596-601
20. Wilbanks A.M., Laporte S.A., Bohn L.M., Barak L.S., and Caron M.G. Apparent loss-of-function mutant GPCR revealed as constitutively desensitized receptors. Biochemistry 41 (2002) 11981-11989
21. Schulz A., and Schöneberg T. The structural evolution of a P2Y-like G-protein-coupled receptor. J. Biol. Chem. 278 (2003) 35531-35541
22. Kostenis E. Is Galpha16 the optimal tool for fishing ligands of orphan G-protein-coupled receptors?. Trends Pharmacol. Sci. 22 (2001) 560-564
23. Scheer A., Fanelli F., Costa T., De Benedetti P.G., and Cotecchia S. The activation process of the alpha1B-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate. Proc. Natl. Acad. Sci. USA 94 (1997) 808-813
24. Jacobs L.L., and Pilbeam D. Of mice and men: fossil-based divergence dates and molecular 'Clocks'. J. Hum. Evol. 9 (1980) 551-555
25. Springer M.S., Murphy W.J., Eizirik E., and O'Brien S.J. Placental mammal diversification and the Cretaceous-Tertiary boundary. Proc. Natl. Acad. Sci. USA 100 (2003) 1056-1061
26. Dubois J.Y., Jekel P.A., Mulder P.P., Bussink A.P., Catzeflis F.M., Carsana A., and Beintema J.J. Pancreatic-type ribonuclease 1 gene duplications in rat species. J. Mol. Evol. 55 (2002) 522-533
27. Barak L.S., Oakley R.H., Laporte S.A., and Caron M.G. Constitutive arrestin-mediated desensitization of a human vasopressin receptor mutant associated with nephrogenic diabetes insipidus. Proc. Natl. Acad. Sci. USA 98 (2001) 93-98
28. Schöneberg T., Schulz A., and Gudermann T. The structural basis of G-protein-coupled receptor function and dysfunction in human diseases. Rev. Physiol. Biochem. Pharmacol. 144 (2002) 143-227
29. Hawtin S.R. Charged residues of the conserved DRY triplet of the vasopressin V1a receptor provide molecular determinants for cell surface delivery and internalization. Mol. Pharmacol. 68 (2005) 1172-1182
30. Schülein R. The early stages of the intracellular transport of membrane proteins: clinical and pharmacological implications. Rev. Physiol. Biochem. Pharmacol. 151 (2004) 45-91
31. Huang S.W., Ardlie K.G., and Yu H.T. Frequency and distribution of t-haplotypes in the Southeast Asian house mouse (Mus musculus castaneus) in Taiwan. Mol. Ecol. 10 (2001) 2349-2354
32. Berridge M.J. Rapid accumulation of inositol trisphosphate reveals that agonists hydrolyse polyphosphoinositides instead of phosphatidylinositol. Biochem. J. 212 (1983) 849-858
33. Schöneberg T., Sandig V., Wess J., Gudermann T., and Schultz G. Reconstitution of mutant V2 vasopressin receptors by adenovirus-mediated gene transfer: molecular basis and clinical implication. J. Clin. Invest. 100 (1997) 1547-1556