메뉴 건너뛰기




Volumn 108, Issue 2, 2015, Pages 272-278

Effect of thanatophoric dysplasia type i mutations on FGFR3 dimerization

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 84921463220     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.11.3460     Document Type: Article
Times cited : (28)

References (39)
  • 1
    • 33644872519 scopus 로고    scopus 로고
    • The new bone biology: Pathologic, molecular, and clinical correlates
    • M.M. Cohen Jr. The new bone biology: pathologic, molecular, and clinical correlates Am. J. Med. Genet. A. 140 2006 2646 2706
    • (2006) Am. J. Med. Genet. A. , vol.140 , pp. 2646-2706
    • Cohen, Jr.M.M.1
  • 2
    • 0037108028 scopus 로고    scopus 로고
    • Some chondrodysplasias with short limbs: Molecular perspectives
    • M.M. Cohen Jr. Some chondrodysplasias with short limbs: molecular perspectives Am. J. Med. Genet. 112 2002 304 313
    • (2002) Am. J. Med. Genet. , vol.112 , pp. 304-313
    • Cohen, Jr.M.M.1
  • 3
    • 0032774475 scopus 로고    scopus 로고
    • Clinical spectrum of fibroblast growth factor receptor mutations
    • M.R. Passos-Bueno, and W.R. Wilcox H. Kitoh Clinical spectrum of fibroblast growth factor receptor mutations Hum. Mutat. 14 1999 115 125
    • (1999) Hum. Mutat. , vol.14 , pp. 115-125
    • Passos-Bueno, M.R.1    Wilcox, W.R.2    Kitoh, H.3
  • 4
    • 0029937714 scopus 로고    scopus 로고
    • Missense FGFR3 mutations create cysteine residues in thanatophoric dwarfism type i (TD1)
    • F. Rousseau, and V. el Ghouzzi J. Bonaventure Missense FGFR3 mutations create cysteine residues in thanatophoric dwarfism type I (TD1) Hum. Mol. Genet. 5 1996 509 512
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 509-512
    • Rousseau, F.1    El Ghouzzi, V.2    Bonaventure, J.3
  • 5
    • 14644394929 scopus 로고    scopus 로고
    • Cell responses to FGFR3 signaling: Growth, differentiation and apoptosis
    • C.G.M. L'Horte, and M.A. Knowles Cell responses to FGFR3 signaling: growth, differentiation and apoptosis Experim. Cell Res. 304 2005 417 431
    • (2005) Experim. Cell Res. , vol.304 , pp. 417-431
    • L'Horte, C.G.M.1    Knowles, M.A.2
  • 6
    • 0028872752 scopus 로고
    • Thanatophoric dysplasia (types i and II) caused by distinct mutations in fibroblast growth factor receptor 3
    • P.L. Tavormina, and R. Shiang J.J. Wasmuth Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3 Nat. Genet. 9 1995 321 328
    • (1995) Nat. Genet. , vol.9 , pp. 321-328
    • Tavormina, P.L.1    Shiang, R.2    Wasmuth, J.J.3
  • 7
    • 0036239904 scopus 로고    scopus 로고
    • Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization
    • R. Adar, and E. Monsonego-Ornan A. Yayon Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization J. Bone Miner. Res. 17 2002 860 868
    • (2002) J. Bone Miner. Res. , vol.17 , pp. 860-868
    • Adar, R.1    Monsonego-Ornan, E.2    Yayon, A.3
  • 8
    • 0031985174 scopus 로고    scopus 로고
    • Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type i
    • P.Y. d'Avis, and S.C. Robertson D.J. Donoghue Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I Cell Growth Differ. 9 1998 71 78
    • (1998) Cell Growth Differ. , vol.9 , pp. 71-78
    • D'Avis, P.Y.1    Robertson, S.C.2    Donoghue, D.J.3
  • 9
    • 58149105445 scopus 로고    scopus 로고
    • Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage
    • P. Krejci, and L. Salazar W.R. Wilcox Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage PLoS ONE 3 2008 e3961 10.1371/journal.pone.0003961
    • (2008) PLoS ONE , vol.3 , pp. e3961
    • Krejci, P.1    Salazar, L.2    Wilcox, W.R.3
  • 10
    • 0029935895 scopus 로고    scopus 로고
    • Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
    • M.C. Naski, and Q. Wang D.M. Ornitz Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia Nat. Genet. 13 1996 233 237
    • (1996) Nat. Genet. , vol.13 , pp. 233-237
    • Naski, M.C.1    Wang, Q.2    Ornitz, D.M.3
  • 11
    • 34249774021 scopus 로고    scopus 로고
    • The localization of FGFR3 mutations causing thanatophoric dysplasia type i differentially affects phosphorylation, processing and ubiquitylation of the receptor
    • J. Bonaventure, W.C. Horne, and R. Baron The localization of FGFR3 mutations causing thanatophoric dysplasia type I differentially affects phosphorylation, processing and ubiquitylation of the receptor FEBS J. 274 2007 3078 3093
    • (2007) FEBS J. , vol.274 , pp. 3078-3093
    • Bonaventure, J.1    Horne, W.C.2    Baron, R.3
  • 13
    • 0029917507 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 3 is a negative regulator of bone growth
    • C. Deng, and A. Wynshaw-Boris P. Leder Fibroblast growth factor receptor 3 is a negative regulator of bone growth Cell 84 1996 911 921
    • (1996) Cell , vol.84 , pp. 911-921
    • Deng, C.1    Wynshaw-Boris, A.2    Leder, P.3
  • 14
    • 84857688284 scopus 로고    scopus 로고
    • Sixteen years and counting: The current understanding of fibroblast growth factor receptor 3 (FGFR3) signaling in skeletal dysplasias
    • S. Foldynova-Trantirkova, W.R. Wilcox, and P. Krejci Sixteen years and counting: the current understanding of fibroblast growth factor receptor 3 (FGFR3) signaling in skeletal dysplasias Hum. Mutat. 33 2012 29 41
    • (2012) Hum. Mutat. , vol.33 , pp. 29-41
    • Foldynova-Trantirkova, S.1    Wilcox, W.R.2    Krejci, P.3
  • 15
    • 84875421249 scopus 로고    scopus 로고
    • Exploring mechanisms of FGF signalling through the lens of structural biology
    • R. Goetz, and M. Mohammadi Exploring mechanisms of FGF signalling through the lens of structural biology Nat. Rev. Mol. Cell Biol. 14 2013 166 180
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 166-180
    • Goetz, R.1    Mohammadi, M.2
  • 16
    • 0033951768 scopus 로고    scopus 로고
    • FGFs, heparan sulfate and FGFRs: Complex interactions essential for development
    • D.M. Ornitz FGFs, heparan sulfate and FGFRs: complex interactions essential for development BioEssays 22 2000 108 112
    • (2000) BioEssays , vol.22 , pp. 108-112
    • Ornitz, D.M.1
  • 17
    • 0035081241 scopus 로고    scopus 로고
    • Fibroblast growth factors
    • D.M. Ornitz, and N. Itoh Fibroblast growth factors Genome Biol. 2 2001 3005
    • (2001) Genome Biol. , vol.2 , pp. 3005
    • Ornitz, D.M.1    Itoh, N.2
  • 18
    • 84865994665 scopus 로고    scopus 로고
    • Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2
    • H. Greulich, and B. Kaplan M. Meyerson Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2 Proc. Natl. Acad. Sci. USA 109 2012 14476 14481
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14476-14481
    • Greulich, H.1    Kaplan, B.2    Meyerson, M.3
  • 19
    • 78650412305 scopus 로고    scopus 로고
    • Targeting RET receptor tyrosine kinase activation in cancer
    • J.E. Phay, and M.H. Shah Targeting RET receptor tyrosine kinase activation in cancer Clin. Cancer Res. 16 2010 5936 5941
    • (2010) Clin. Cancer Res. , vol.16 , pp. 5936-5941
    • Phay, J.E.1    Shah, M.H.2
  • 20
    • 84875378602 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor-3 in urothelial tumorigenesis
    • G. Iyer, and M.I. Milowsky Fibroblast growth factor receptor-3 in urothelial tumorigenesis Urol. Oncol. 31 2013 303 311
    • (2013) Urol. Oncol. , vol.31 , pp. 303-311
    • Iyer, G.1    Milowsky, M.I.2
  • 21
    • 77949371562 scopus 로고    scopus 로고
    • Measuring the energetics of membrane protein dimerization in mammalian membranes
    • L. Chen, and L. Novicky K. Hristova Measuring the energetics of membrane protein dimerization in mammalian membranes J. Am. Chem. Soc. 132 2010 3628 3635
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3628-3635
    • Chen, L.1    Novicky, L.2    Hristova, K.3
  • 22
    • 78649854195 scopus 로고    scopus 로고
    • The extracellular domain of fibroblast growth factor receptor 3 inhibits ligand-independent dimerization
    • L. Chen, and J. Placone K. Hristova The extracellular domain of fibroblast growth factor receptor 3 inhibits ligand-independent dimerization Sci. Signal. 3 2010 ra86
    • (2010) Sci. Signal. , vol.3 , pp. ra86
    • Chen, L.1    Placone, J.2    Hristova, K.3
  • 23
    • 84869435127 scopus 로고    scopus 로고
    • Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions
    • N. Del Piccolo, and J. Placone K. Hristova Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions Anal. Chem. 84 2012 8650 8655
    • (2012) Anal. Chem. , vol.84 , pp. 8650-8655
    • Del Piccolo, N.1    Placone, J.2    Hristova, K.3
  • 24
    • 84893162386 scopus 로고    scopus 로고
    • Uninduced high-yield bacterial expression of fluorescent proteins
    • S. Sarabipour, C. King, and K. Hristova Uninduced high-yield bacterial expression of fluorescent proteins Anal. Biochem. 449 2014 155 157
    • (2014) Anal. Biochem. , vol.449 , pp. 155-157
    • Sarabipour, S.1    King, C.2    Hristova, K.3
  • 25
    • 49449093799 scopus 로고    scopus 로고
    • Quantitative measurements of protein interactions in a crowded cellular environment
    • E. Li, and J. Placone K. Hristova Quantitative measurements of protein interactions in a crowded cellular environment Anal. Chem. 80 2008 5976 5985
    • (2008) Anal. Chem. , vol.80 , pp. 5976-5985
    • Li, E.1    Placone, J.2    Hristova, K.3
  • 26
    • 0018650688 scopus 로고
    • An analytic solution to the Förster energy transfer problem in two dimensions
    • P.K. Wolber, and B.S. Hudson An analytic solution to the Förster energy transfer problem in two dimensions Biophys. J. 28 1979 197 210
    • (1979) Biophys. J. , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 27
    • 84896501967 scopus 로고    scopus 로고
    • The FRET signatures of noninteracting proteins in membranes: Simulations and experiments
    • C. King, and S. Sarabipour K. Hristova The FRET signatures of noninteracting proteins in membranes: simulations and experiments Biophys. J. 106 2014 1309 1317
    • (2014) Biophys. J. , vol.106 , pp. 1309-1317
    • King, C.1    Sarabipour, S.2    Hristova, K.3
  • 28
    • 33750728028 scopus 로고    scopus 로고
    • Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers
    • T.H. Evers, and E.M.W.M. van Dongen M. Merkx Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers Biochemistry 45 2006 13183 13192
    • (2006) Biochemistry , vol.45 , pp. 13183-13192
    • Evers, T.H.1    Van Dongen, E.M.W.M.2    Merkx, M.3
  • 30
    • 0017139396 scopus 로고
    • Plasma membrane vesiculation: A new technique for isolation of plasma membranes
    • R.E. Scott Plasma membrane vesiculation: a new technique for isolation of plasma membranes Science 194 1976 743 745
    • (1976) Science , vol.194 , pp. 743-745
    • Scott, R.E.1
  • 31
    • 0018331203 scopus 로고
    • Plasma membrane vesiculation in 3T3 and SV3T3 cells. II. Factors affecting the process of vesiculation
    • R.E. Scott, and P.B. Maercklein Plasma membrane vesiculation in 3T3 and SV3T3 cells. II. Factors affecting the process of vesiculation J. Cell Sci. 35 1979 245 252
    • (1979) J. Cell Sci. , vol.35 , pp. 245-252
    • Scott, R.E.1    Maercklein, P.B.2
  • 32
    • 0018331202 scopus 로고
    • Plasma membrane vesiculation in 3T3 and SV3T3 cells. I. Morphological and biochemical characterization
    • R.E. Scott, and R.G. Perkins P.B. Maercklein Plasma membrane vesiculation in 3T3 and SV3T3 cells. I. Morphological and biochemical characterization J. Cell Sci. 35 1979 229 243
    • (1979) J. Cell Sci. , vol.35 , pp. 229-243
    • Scott, R.E.1    Perkins, R.G.2    Maercklein, P.B.3
  • 33
    • 84867327158 scopus 로고    scopus 로고
    • Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET
    • J. Placone, and K. Hristova Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET PLoS ONE 7 2012 e46678
    • (2012) PLoS ONE , vol.7 , pp. e46678
    • Placone, J.1    Hristova, K.2
  • 34
    • 84903772158 scopus 로고    scopus 로고
    • Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes
    • J. Placone, and L. He K. Hristova Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes Biochim. Biophys. Acta 1838 2014 2326 2330
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2326-2330
    • Placone, J.1    He, L.2    Hristova, K.3
  • 35
    • 84877024051 scopus 로고    scopus 로고
    • Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells
    • S. Sarabipour, and K. Hristova Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells Biochim. Biophys. Acta 1828 2013 1829 1833
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1829-1833
    • Sarabipour, S.1    Hristova, K.2
  • 36
    • 84879836173 scopus 로고    scopus 로고
    • FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain
    • S. Sarabipour, and K. Hristova FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain Biophys. J. 105 2013 165 171
    • (2013) Biophys. J. , vol.105 , pp. 165-171
    • Sarabipour, S.1    Hristova, K.2
  • 37
    • 0020106881 scopus 로고
    • Quantitative characterization of the lateral distribution of membrane proteins within the lipid bilayer
    • E. Freire, and B. Snyder Quantitative characterization of the lateral distribution of membrane proteins within the lipid bilayer Biophys. J. 37 1982 617 624
    • (1982) Biophys. J. , vol.37 , pp. 617-624
    • Freire, E.1    Snyder, B.2
  • 38
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • S.F. Betz Disulfide bonds and the stability of globular proteins Protein Sci. 2 1993 1551 1558
    • (1993) Protein Sci. , vol.2 , pp. 1551-1558
    • Betz, S.F.1
  • 39
    • 37548998932 scopus 로고    scopus 로고
    • Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain
    • A. McAuley, and J. Jacob M. Matsumura Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain Protein Sci. 17 2008 95 106
    • (2008) Protein Sci. , vol.17 , pp. 95-106
    • McAuley, A.1    Jacob, J.2    Matsumura, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.