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Volumn 427, Issue 8, 2015, Pages 1705-1714

FGFR3 unliganded dimer stabilization by the juxtamembrane domain

Author keywords

Juxtamembrane domain; Membrane protein dimerization; Receptor tyrosine kinases; Thermodynamics; Transmembrane domain

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR 3; GLYCOPHORIN A; FGFR3 PROTEIN, HUMAN; SIGNAL PEPTIDE;

EID: 84933041582     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.02.013     Document Type: Article
Times cited : (34)

References (44)
  • 2
    • 33751328082 scopus 로고    scopus 로고
    • ErbB receptors: New insights on mechanisms and biology
    • Linggi B, Carpenter G. ErbB receptors: new insights on mechanisms and biology. Trends Cell Biol 2006;16:649-56.
    • (2006) Trends Cell Biol , vol.16 , pp. 649-656
    • Linggi, B.1    Carpenter, G.2
  • 3
    • 1842471336 scopus 로고    scopus 로고
    • Signaling through the epidermal growth factor receptor during the development of malignancy
    • Grandis JR, Sok JC. Signaling through the epidermal growth factor receptor during the development of malignancy. Pharmacol Ther 2004;102:37-46.
    • (2004) Pharmacol Ther , vol.102 , Issue.37-46
    • Grandis, J.R.1    Sok, J.C.2
  • 5
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010;141:1117-34.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 6
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2000;103:211-25.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 8
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger J. Common and distinct elements in cellular signaling via EGF and FGF receptors. Science 2004;306: 1506-7.
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 9
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang XW, Gureasko J, Shen K, Cole PA, Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006;125:1137-49.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.W.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 11
    • 84873280409 scopus 로고    scopus 로고
    • Conformational coupling across the plasma membrane in activation of the EGF receptor
    • Endres NF,Das R, SmithAW, Arkhipov A, Kovacs E, Huang YJ, et al. Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 2013;152:543-56.
    • (2013) Cell , vol.152 , pp. 543-556
    • Endres Nfdas, R.1    Smithaw Arkhipov, A.2    Kovacs, E.3    Huang, Y.J.4
  • 12
    • 78651372868 scopus 로고    scopus 로고
    • Nerve growth factor receptor TrkA exists as a preformed, yet inactive, dimer in living cells
    • Shen JY, Maruyama IN. Nerve growth factor receptor TrkA exists as a preformed, yet inactive, dimer in living cells. FEBS Lett 2011;585:295-9.
    • (2011) FEBS Lett , vol.585 , pp. 295-299
    • Shen, J.Y.1    Maruyama, I.N.2
  • 13
    • 84933063233 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells
    • Maruyama I, Shen JY. Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells. FASEB J 2012;26:971.8.
    • (2012) FASEB J , vol.26 , pp. 9718
    • Maruyama, I.1    Shen, J.Y.2
  • 15
    • 84868618665 scopus 로고    scopus 로고
    • Grb2, a double-edged sword of receptor tyrosine kinase signaling
    • Belov AA, Mohammadi M. Grb2, a double-edged sword of receptor tyrosine kinase signaling. Sci Signal 2012;5:pe49.
    • (2012) Sci Signal , vol.5 , pp. pe49
    • Belov, A.A.1    Mohammadi, M.2
  • 16
    • 84857640514 scopus 로고    scopus 로고
    • Physical-chemical principles underlying RTK activation, and their implications for human disease
    • He L, Hristova K. Physical-chemical principles underlying RTK activation, and their implications for human disease. Biochim Biophys Acta 2012;1818:995-1005.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 995-1005
    • He, L.1    Hristova, K.2
  • 17
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • Li E, Hristova K. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry 2006;45:6241-51.
    • (2006) Biochemistry , vol.45 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 18
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N, Endres NF, Engel K, Deindl S, Das R, Lamers MH, et al. Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 2009;137: 1293-307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5    Lamers, M.H.6
  • 20
    • 0034464005 scopus 로고    scopus 로고
    • The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans
    • Vajo Z, Francomano CA, Wilkin DJ. The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: the achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans. Endocr Rev 2000;21:23-39.
    • (2000) Endocr Rev , vol.21 , pp. 23-39
    • Vajo, Z.1    Francomano, C.A.2    Wilkin, D.J.3
  • 22
    • 0028793472 scopus 로고
    • Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans
    • Meyers GA, Orlow SJ, Munro IR, Przylepa KA, Jabs EW. Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans. Nat Genet 1995;11:462-4.
    • (1995) Nat Genet , vol.11 , pp. 462-464
    • Meyers, G.A.1    Orlow, S.J.2    Munro, I.R.3    Przylepa, K.A.4    Jabs, E.W.5
  • 23
    • 0030941036 scopus 로고    scopus 로고
    • Activation of FGF receptors by mutations in the transmembrane domain
    • Li Y, Mangasarian K, Mansukhani A, Basilico C. Activation of FGF receptors by mutations in the transmembrane domain. Oncogene 1997;14:1397-406.
    • (1997) Oncogene , vol.14 , pp. 1397-1406
    • Li, Y.1    Mangasarian, K.2    Mansukhani, A.3    Basilico, C.4
  • 24
    • 77956907848 scopus 로고    scopus 로고
    • The physical basis behind achondroplasia, the most common form of human dwarfism
    • He L, Horton WA, Hristova K. The physical basis behind achondroplasia, the most common form of human dwarfism. J Biol Chem 2010;285:30103-14.
    • (2010) J Biol Chem , vol.285 , pp. 30103-30114
    • He, L.1    Horton, W.A.2    Hristova, K.3
  • 25
    • 84859976618 scopus 로고    scopus 로고
    • Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation
    • He LJ, Serrano C, Niphadkar N, Shobnam N, Hristova K. Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation. PLoS One 2012;7:e34808.
    • (2012) PLoS One , vol.7 , pp. e34808
    • He, L.J.1    Serrano, C.2    Niphadkar, N.3    Shobnam, N.4    Hristova, K.5
  • 26
    • 84874269934 scopus 로고    scopus 로고
    • Multiple consequences of a single amino acid pathogenic RTK mutation: The A391E mutation in FGFR3
    • Chen F, Sarabipour S, Hristova K. Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3. PLoS One 2013;8:e56521.
    • (2013) PLoS One , vol.8 , pp. e56521
    • Chen, F.1    Sarabipour, S.2    Hristova, K.3
  • 27
    • 78649854195 scopus 로고    scopus 로고
    • The extracellular domain of fibroblast growth factor receptor 3 inhibits ligandindependent dimerization
    • Chen L, Placone J, Novicky L, Hristova K. The extracellular domain of fibroblast growth factor receptor 3 inhibits ligandindependent dimerization. Sci Signal 2010;3:ra86.
    • (2010) Sci Signal , vol.3 , pp. ra86
    • Chen, L.1    Placone, J.2    Novicky, L.3    Hristova, K.4
  • 28
    • 33750728028 scopus 로고    scopus 로고
    • Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers
    • Evers TH, van Dongen EMWM, Faesen AC, Meijer EW, Merkx M. Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers. Biochemistry 2006;45:13183-92.
    • (2006) Biochemistry , vol.45 , pp. 13183-13192
    • Evers, T.H.1    Van Dongen, E.M.W.M.2    Faesen, A.C.3    Meijer, E.W.4    Merkx, M.5
  • 29
    • 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
    • Del Piccolo N, Placone J, He L, Agudelo SC, Hristova K. 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 2012;84:8650-5.
    • (2012) Anal Chem , vol.84 , pp. 8650-8655
    • Del Piccolo, N.1    Placone, J.2    He, L.3    Agudelo, S.C.4    Hristova, K.5
  • 30
    • 77949371562 scopus 로고    scopus 로고
    • Measuring the energetics of membrane protein dimerization in mammalian membranes
    • Chen L, Novicky L, Merzlyakov M, Hristov T, Hristova K. Measuring the energetics of membrane protein dimerization in mammalian membranes. J Am Chem Soc 2010;132: 3628-35.
    • (2010) J Am Chem Soc , vol.132 , pp. 3628-3635
    • Chen, L.1    Novicky, L.2    Merzlyakov, M.3    Hristov, T.4    Hristova, K.5
  • 31
    • 0018331203 scopus 로고
    • Plasma-membrane vesiculation in 3T3 cells and Sv3T3 cells. 2. Factors affecting the process of vesiculation
    • Scott RE, Maercklein PB. Plasma-membrane vesiculation in 3T3 cells and Sv3T3 cells. 2. Factors affecting the process of vesiculation. J Cell Sci 1979;35:245-52.
    • (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 cells and Sv3T3 cells. 1. Morphological and biochemical characterization
    • Scott RE, Perkins RG, Zschunke MA, Hoerl BJ, Maercklein PB. Plasma-membrane vesiculation in 3T3 cells and Sv3T3 cells. 1. Morphological and biochemical characterization. J Cell Sci 1979;35:229-43.
    • (1979) J Cell Sci , vol.35 , pp. 229-243
    • Scott, R.E.1    Perkins, R.G.2    Zschunke, M.A.3    Hoerl, B.J.4    Maercklein, P.B.5
  • 33
    • 0017139396 scopus 로고
    • Plasma membrane vesiculation: A new technique for isolation of plasma membrane
    • Scott RE. Plasma membrane vesiculation: a new technique for isolation of plasma membrane. Science 1976;194:743-5.
    • (1976) Science , vol.194 , pp. 743-745
    • Scott, R.E.1
  • 35
    • 79960590320 scopus 로고    scopus 로고
    • Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments
    • Hong H, Bowie JU. Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments. J Am Chem Soc 2011;133:11389-98.
    • (2011) J Am Chem Soc , vol.133 , pp. 11389-11398
    • Hong, H.1    Bowie, J.U.2
  • 36
    • 84879836173 scopus 로고    scopus 로고
    • FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain
    • Sarabipour S, Hristova K. FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain. Biophys J 2013;105:165-71.
    • (2013) Biophys J , vol.105 , pp. 165-171
    • Sarabipour, S.1    Hristova, K.2
  • 37
    • 0033544892 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the receptor for epidermal growth factor containing the membrane-spanning segment in response to treatment with epidermal growth factor
    • Tanner KG, Kyte J. Dimerization of the extracellular domain of the receptor for epidermal growth factor containing the membrane-spanning segment in response to treatment with epidermal growth factor. J Biol Chem 1999;274:35985-90.
    • (1999) J Biol Chem , vol.274 , pp. 35985-35990
    • Tanner, K.G.1    Kyte, J.2
  • 39
    • 84870823045 scopus 로고    scopus 로고
    • Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence
    • He L, Hristova K. Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence. Sci Rep 2012;2:854.
    • (2012) Sci Rep , vol.2 , pp. 854
    • He, L.1    Hristova, K.2
  • 40
    • 0034213931 scopus 로고    scopus 로고
    • RTK mutations and human syndromes-when good receptors turn bad
    • Robertson SC, Tynan JA, Donoghue DJ. RTK mutations and human syndromes-when good receptors turn bad. Trends Genet 2000;16:265-71.
    • (2000) Trends Genet , vol.16 , pp. 265-271
    • Robertson, S.C.1    Tynan, J.A.2    Donoghue, D.J.3
  • 41
    • 0030969251 scopus 로고    scopus 로고
    • Transmembrane domain sequence requirements for activation of the p185(c-neu) receptor tyrosine kinase
    • Chen LI, Webster MK, Meyer AN, Donoghue DJ. Transmembrane domain sequence requirements for activation of the p185(c-neu) receptor tyrosine kinase. J Cell Biol 1997;137: 619-31.
    • (1997) J Cell Biol , vol.137 , pp. 619-631
    • Chen, L.I.1    Webster, M.K.2    Meyer, A.N.3    Donoghue, D.J.4
  • 42
    • 0030064347 scopus 로고    scopus 로고
    • Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia
    • Webster MK, Donoghue DJ. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia. EMBO J 1996;15:520-7.
    • (1996) EMBO J , vol.15 , pp. 520-527
    • Webster, M.K.1    Donoghue, D.J.2
  • 43
    • 84893162386 scopus 로고    scopus 로고
    • Un-induced high-yield bacterial expression of fluorescent proteins
    • Sarabipour S, King C, Hristova K. Un-induced high-yield bacterial expression of fluorescent proteins. Anal Biochem 2014;449:155-7.
    • (2014) Anal Biochem , vol.449 , pp. 155-157
    • Sarabipour, S.1    King, C.2    Hristova, K.3
  • 44
    • 49449093799 scopus 로고    scopus 로고
    • Quantitative measurements of protein interactions in a crowded cellular environment
    • Li E, Placone J, Merzlyakov M, Hristova K. Quantitative measurements of protein interactions in a crowded cellular environment. Anal Chem 2008;80:5976-85.
    • (2008) Anal Chem , vol.80 , pp. 5976-5985
    • Li, E.1    Placone, J.2    Merzlyakov, M.3    Hristova, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.