A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia

Physiological Genomics

Volumn 2000, Issue 2, 2000, Pages 9-12

  Winterpacht, Andreas ^a,b   Hilbert, Katja ^a   Stelzer, Christiane ^a   Schweikardt, Thorsten ^a   Decker, Heinz ^a   Segerer, Hugo ^c   Spranger, Jürgen ^a   Zabel, Bernhard ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

^b UNIVERSITY OF HAMBURG   (Germany)

^c Children's Hospital St Hedwig Regensburg   (Germany)

Author keywords

Chondrodysplasia; Glycoprotein; Glycosylation; Tyrosine kinase receptor

Indexed keywords

DNA; FGFR3 PROTEIN, HUMAN; FGFR3 PROTEIN, MOUSE; FIBROBLAST GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 3; PROTEIN TYROSINE KINASE;

AMINO ACID SUBSTITUTION; ANIMAL; ARTICLE; BINDING SITE; C57BL MOUSE; CASE REPORT; CHEMISTRY; CHONDRODYSPLASIA; FEMALE; GENETICS; GLYCOSYLATION; HUMAN; INFANT; METABOLISM; MOUSE; MUTATION; NUCLEOTIDE SEQUENCE; PATHOLOGY; POINT MUTATION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; BINDING SITES; DNA; DNA MUTATIONAL ANALYSIS; FEMALE; GLYCOSYLATION; HUMANS; INFANT; MICE; MICE, INBRED C57BL; MUTATION; OSTEOCHONDRODYSPLASIAS; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE KINASES; RECEPTOR, FIBROBLAST GROWTH FACTOR, TYPE 3; RECEPTORS, FIBROBLAST GROWTH FACTOR;

EID: 0034707489     PISSN: 15312267     EISSN: None     Source Type: Journal    
DOI: 10.1152/physiolgenomics.2000.2.1.9     Document Type: Article

References (27)

1. Bellus, G. A., I. McIntosh, E. A. Smith, A. S. Aylsworth, I. Kaitila, W. A. Horton, G. A. Greenhaw, et al. A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia. Nat. Genet. 10: 357-359, 1995.
2. Bhatia, P. K., and A. Mukhopadhyay. Protein glycosylation: implications for in vivo functions and therapeutic applications. Adv. Biochem. Eng. Biotechnol. 64: 155-201, 1998.
3. Gray, T. E., M. Eisenstein, T. Shimon, D. Givol, and A. Yayon. Molecular modeling based mutagenesis defines ligand binding and specificity determining regions of fibroblast growth factor receptors. Biochemistry 34: 10325-10333, 1995.
4. Grigeliogniené, G., L. Hagenäs, O. Eklöf, L. Neumeyer, P. E. Haereid, and M. Anvret. A novel missense mutation Ile538Val in the fibroblast growth factor receptor 3 in hypochondroplasia. Human Mutation, Mutation in Brief, 122 Online, 1997.
5. Harpaz, Y., and C. Chothia. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238: 528-539, 1994.
6. Hilbert, M., K. Hilbert, J. Spranger, G. Wildhardt, A. Winterpacht, C. Wüchner, and B. Zabel. Hypochondroplasie, Achondroplasie und thanatophore Dysplasie als Folge von Mutationen des Fibroblastenwachstumsfaktorrezeptor-3-Gens (FGFR3). Monatsschr. Kinderheilkd. 146: 687-691, 1998.
7. Johnson, D. E., and L. T. Williams. Structural and functional diversity in the FGF receptor multigene family. Adv. Cancer Res. 60: 1-40, 1993.
8. Kanai, M., M. Göke, S. Tsunekawa, and D. K. Podolsky. Signal transduction pathway of human fibroblast growth factor receptor 3. J. Biol. Chem. 272: 6621-6628, 1997.
9. Keegan, K., D. E. Johnson, L. T. Williams, and M. Hayman. Isolation of an additional member of the fibroblast growth factor receptor family, FGFR3. Proc. Natl. Acad. Sci. USA 88: 1095-1099. 1991.
10. Keegan, K., S. Meyer, and M. J. Hayman. Structural and biosynthetic characterization of fibroblast growth factor receptor 3 (FGFR-3) protein. Oncogene 2: 2229-2236. 1991.
11. Lonnqvist, L., L. Karttunen, T. Rantamaki, C. Kielty, M. Raghunath, and L. Peltonen. A point mutation creating an extra N-glycosylation site in fibrillin-1 results in neonatal Marfan syndrome. Genomics 36: 468-75, 1998.
12. Mangasarian, K., Y. Li, A. Mansukhani, and C. Basilico. Mutation associated with Crouzon syndrome causes ligand-independent dimerization and activation of FGF receptor-2. J. Cell. Physiol. 172: 117-125, 1997.
13. McKeehan, W. L., F. Wang, and M. Kann. The heparan sulfate-fibroblast growth factor family: diversity of structure and function. Progr. Nucleic Acid Res. Mol. Biol. 59: 135-176, 1998.
14. Murgue, B., S. Tsunekawa, I. Rosenberg, M. deBeaumont, and D. K. Podolsky. Identification of a novel variant form of fibroblast growth factor receptor 3 (FGFR3 IIIb) in human colonic epithelium. Cancer Res. 54: 5206-5211, 1994.
15. Naski, M. C., Q. Wang, J. Xu, and D. M. Ornitz. Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia. Nat. Genet. 13: 233-237, 1996.
16. Pariyarath, R., F. Pagani, C. Stuani, R. Garcia, and F. E. Baralle. L273S missense substitution in human lysosomal acid lipase creates a new N-glycosylation site. FEBS Lett. 397: 79-82, 1996.
17. Plotnikov, N., J. Schlessinger, S. R. Hubbard, and M. Mohammadi. Structural basis for FGF receptor dimerization and activation. Cell 98: 641-650, 1999.
18. Prinos, P., T. Costa, A. Sommer, M. W. Kilpatrick, and P. Tsipouras. A common FGFR3 gene mutation in hypochondroplasia. Hum. Mol. Genet. 4: 2097-2101, 1995.
19. Raffioni, S., Y.-Z. Zhu, R. A. Bradshaw, and L. M. Thompson. Effect of transmembrane and kinase domain mutations on fibroblast growth factor receptor 3 chimera signaling in PC12 cells. J. Biol. Chem. 52: 35250-35259, 1998.
20. Ricketts, M. H., D. Goldman, J. C. Long, and P. Manowitz. Arylsulfatase A pseudodeficiency-associated mutations: population studies and identification of a novel haplotype. Am. J. Med. Genet. 67: 387-92, 1996.
21. Rousseau, F., J. Bonaventure, L. Legeai-Mallet, H. Schmidt, J. Weissenbach, P. Maroteaux, A. Munnich, and M. Le Merrer. Clinical and genetic heterogeneity of hypochondroplasia. J. Med. Genet. 33: 749-752, 1996.
22. Sali, A., and T. L. Blundell. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234: 779-815, 1993.
23. Su, W.-C. S., M. Kitagawa, N. Xue, B. Xie, S. Garofalo, J. Cho, C. Deng, et al. Activation of Stat1 by mutant fibroblast growth-factor receptor in thanatophoric dysplasia type II dwarfism. Nature 386: 287-292, 1997.
24. Webster, M. K., and D. J. Donoghue. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia. EMBO J. 15: 520-527, 1996.
25. Webster, M. K., and B. J. Donoghue. FGFR activation in skeletal disorders: too much of a good thing. Trends Genet. 13: 178-182, 1997.
26. Wilkie, A. O. M., G. M. Morriss-Kay, E. Y. Jones, and J. K. Heath. Functions of fibroblast growth factors and their receptors. Curr. Biol. 5: 500-507, 1995.
27. Wüchner, C., K. Hilbert, B. Zabel, and A. Winterpacht. Human fibroblast growth factor receptor 3 gene (FGFR3) genomic sequence and primer set information for gene analysis. Hum. Genet. 100: 215-219, 1997.