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Volumn 40, Issue 11, 2008, Pages 2649-2659

Transient dimerization and interaction with ERGIC-53 occur in the fibroblast growth factor receptor 3 early secretory pathway

Author keywords

ERGIC 53; FGFR3; Quality control; Secretory pathway

Indexed keywords

ENDOPLASMIC RETICULUM GOLGI COMPLEX INTERMEDIATE COMPARTMENT 53 PROTEIN; FIBROBLAST GROWTH FACTOR RECEPTOR 3; MANNOSE; MANNOSE BINDING LECTIN; MONOMER; MUTANT PROTEIN; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 48349146353     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.05.017     Document Type: Article
Times cited : (8)

References (32)
  • 2
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C., and Hauri H.P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. Journal of Cell Science 119 (2006) 2173-2183
    • (2006) Journal of Cell Science , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 6
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: quality control in the secretory pathway
    • Ellgaard L., Molinari M., and Helenius A. Setting the standards: quality control in the secretory pathway. Science 286 (1999) 1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 7
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 8
    • 33947331068 scopus 로고    scopus 로고
    • FGFR3 intracellular mutations induce tyrosine phosphorylation in the Golgi and defective glycosylation
    • Gibbs L., and Legai-Mallet L. FGFR3 intracellular mutations induce tyrosine phosphorylation in the Golgi and defective glycosylation. Biochimica et Biophysica Acta 4 (2007) 502-512
    • (2007) Biochimica et Biophysica Acta , vol.4 , pp. 502-512
    • Gibbs, L.1    Legai-Mallet, L.2
  • 9
    • 0032433851 scopus 로고    scopus 로고
    • The curious state of the Golgi apparatus
    • Glick B.S., and Malhotra V. The curious state of the Golgi apparatus. Cell 95 (1998) 883-889
    • (1998) Cell , vol.95 , pp. 883-889
    • Glick, B.S.1    Malhotra, V.2
  • 10
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annual Review of Biochemistry 73 (2004) 1019-1049
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 11
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell 100 (2000) 113-127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 12
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC53 is a functional mannose selective and calcium-dependent human homologue of leguminous lectins
    • Itin C., Roche A.C., Monsigny M., and Hauri H.P. ERGIC53 is a functional mannose selective and calcium-dependent human homologue of leguminous lectins. Molecular Biology of the Cell 7 (1996) 483-493
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 483-493
    • Itin, C.1    Roche, A.C.2    Monsigny, M.3    Hauri, H.P.4
  • 13
    • 0027192075 scopus 로고
    • An essential heparin-binding domain in the fibroblast growth factor receptor kinase
    • Kan M., Wang F., Xu J., Crabb J.W., Hou J., and McKeehan W.L. An essential heparin-binding domain in the fibroblast growth factor receptor kinase. Science 259 (1993) 1918-1921
    • (1993) Science , vol.259 , pp. 1918-1921
    • Kan, M.1    Wang, F.2    Xu, J.3    Crabb, J.W.4    Hou, J.5    McKeehan, W.L.6
  • 14
    • 1342332090 scopus 로고    scopus 로고
    • Mutant frizzled 4 associated with vitreoretinophaty traps wild-type Frizzled in the endoplasmic reticulum by oligomerization
    • Kaykas A., Yang-Snyder J., Héroux M., Shah K.V., Bouvier M., and Moon R.T. Mutant frizzled 4 associated with vitreoretinophaty traps wild-type Frizzled in the endoplasmic reticulum by oligomerization. Nature Cell Biology 6 (2004) 52-58
    • (2004) Nature Cell Biology , vol.6 , pp. 52-58
    • Kaykas, A.1    Yang-Snyder, J.2    Héroux, M.3    Shah, K.V.4    Bouvier, M.5    Moon, R.T.6
  • 15
    • 0026335813 scopus 로고
    • Structural and biosynthetic characterization of the FGFR3 protein
    • Keegan K., Meyer S., and Hayman M.J. Structural and biosynthetic characterization of the FGFR3 protein. Oncogene 6 (1991) 2229-2236
    • (1991) Oncogene , vol.6 , pp. 2229-2236
    • Keegan, K.1    Meyer, S.2    Hayman, M.J.3
  • 16
    • 0026561901 scopus 로고
    • Brefeldin A: insight into the control of membrane traffic and organelle structure
    • Klausner R.D., Donaldson J.G., and Lippincott-Schwartz J. Brefeldin A: insight into the control of membrane traffic and organelle structure. Journal of Cell Biology 116 (1992) 1071-1080
    • (1992) Journal of Cell Biology , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 17
    • 0038607097 scopus 로고    scopus 로고
    • The thanatophoric dysplasia type II mutation hampers complete maturation of fibroblast growth factor receptor 3 (FGFR3) which activates signal transducer and activator of transcription 1 (STAT1) from the endoplasmic reticulum
    • Lievens P.M.-J., and Liboi E. The thanatophoric dysplasia type II mutation hampers complete maturation of fibroblast growth factor receptor 3 (FGFR3) which activates signal transducer and activator of transcription 1 (STAT1) from the endoplasmic reticulum. Journal of Biological Chemistry 278 (2003) 17344-17349
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 17344-17349
    • Lievens, P.M.-J.1    Liboi, E.2
  • 18
    • 5644241730 scopus 로고    scopus 로고
    • The kinase activity of fibroblast growth factor receptor 3 with activation loop mutations affects receptor trafficking and signaling
    • Lievens P.M.-J., Mutinelli C., Baynes D., and Liboi E. The kinase activity of fibroblast growth factor receptor 3 with activation loop mutations affects receptor trafficking and signaling. Journal of Biological Chemistry 279 (2004) 43254-43260
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 43254-43260
    • Lievens, P.M.-J.1    Mutinelli, C.2    Baynes, D.3    Liboi, E.4
  • 19
    • 33644956734 scopus 로고    scopus 로고
    • K644E/M FGFR3 mutants activate Erk1/2 from the Endoplasmic Reticulum through FRS2α and PLCγ-independent pathways
    • Lievens P.M.-J., Roncador A., and Liboi E. K644E/M FGFR3 mutants activate Erk1/2 from the Endoplasmic Reticulum through FRS2α and PLCγ-independent pathways. Journal of Molecular Biology 357 (2006) 783-792
    • (2006) Journal of Molecular Biology , vol.357 , pp. 783-792
    • Lievens, P.M.-J.1    Roncador, A.2    Liboi, E.3
  • 20
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J., Donaldson J.G., Schweizer A., Berger E.G., Hauri H.P., Yuan L.P., et al. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60 (1990) 821-836
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.P.6
  • 21
    • 48249131211 scopus 로고    scopus 로고
    • The cargo receptors Surf4, endoplasmic reticulum-golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and golgi
    • Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., and Hauri H.P. The cargo receptors Surf4, endoplasmic reticulum-golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and golgi. Molecular Biology of the Cell 5 (2008) 1976-1990
    • (2008) Molecular Biology of the Cell , vol.5 , pp. 1976-1990
    • Mitrovic, S.1    Ben-Tekaya, H.2    Koegler, E.3    Gruenberg, J.4    Hauri, H.P.5
  • 22
    • 0032704952 scopus 로고    scopus 로고
    • Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII
    • Moussalli M., Pipe S.W., Hauri H.P., Nichols W.C., Ginsburg D., and Kaufman R.J. Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII. Journal of Biological Chemistry 274 (1999) 32539-32542
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 32539-32542
    • Moussalli, M.1    Pipe, S.W.2    Hauri, H.P.3    Nichols, W.C.4    Ginsburg, D.5    Kaufman, R.J.6
  • 23
    • 0032478548 scopus 로고    scopus 로고
    • Mutations in the ER-Golgi intermadiate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII
    • Nichols W.C., Seligsohn U., Zivelin A., Terry V.E., Hertel C.E., Wheatley M.A., et al., Hauri H.P., Kaufman R.J. Mutations in the ER-Golgi intermadiate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII. Cell 93 (1998) 61-70
    • (1998) Cell , vol.93 , pp. 61-70
    • Nichols, W.C.1    Seligsohn, U.2    Zivelin, A.3    Terry, V.E.4    Hertel, C.E.5    Wheatley, M.A.6
  • 25
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116 (2000) 191-203
    • (2000) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 26
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov A.N., Schlessinger J., Hubbard S.R., and Mohammadi M. Structural basis for FGF receptor dimerization and activation. Cell 98 (1999) 641-650
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 27
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste J., and Svensson K. Distribution of the intermediate elements operating in ER to Golgi transport. Journal of Cell Science 100 (1991) 415-430
    • (1991) Journal of Cell Science , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 28
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 103 (2000) 211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 30
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 31
    • 0031661435 scopus 로고    scopus 로고
    • Fibroblast growth factors as multifunctional signaling factors
    • Szebenyi G., and Fallon J.F. Fibroblast growth factors as multifunctional signaling factors. International Review of Cytology 185 (1999) 45-106
    • (1999) International Review of Cytology , vol.185 , pp. 45-106
    • Szebenyi, G.1    Fallon, J.F.2
  • 32
    • 0030331567 scopus 로고    scopus 로고
    • Activin receptors: cellular signalling by receptor serine kinases
    • Zimmerman C.M., and Mathews L.S. Activin receptors: cellular signalling by receptor serine kinases. Biochemical Society Symposia 62 (1996) 25-38
    • (1996) Biochemical Society Symposia , vol.62 , pp. 25-38
    • Zimmerman, C.M.1    Mathews, L.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.