메뉴 건너뛰기




Volumn 1804, Issue 4, 2010, Pages 856-865

Rescue of F508del-CFTR by RXR motif inactivation triggers proteome modulation associated with the unfolded protein response

Author keywords

CFTR; Cystic fibrosis; Protein trafficking; RXR motif; Therapeutic target; Unfolded protein response

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN; PROTEOME; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 76849090407     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.12.013     Document Type: Article
Times cited : (30)

References (58)
  • 1
    • 0023648813 scopus 로고
    • A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene
    • Dorin J.R., Novak M., Hill R.E., Brock D.J., Secher D.S., and van Heyningen V. A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene. Nature 326 (1987) 614-617
    • (1987) Nature , vol.326 , pp. 614-617
    • Dorin, J.R.1    Novak, M.2    Hill, R.E.3    Brock, D.J.4    Secher, D.S.5    van Heyningen, V.6
  • 3
    • 0025155528 scopus 로고
    • Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells
    • Rich D.P., Anderson M.P., Gregory R.J., Cheng S.H., Paul S., Jefferson D.M., McCann J.D., Klinger K.W., Smith A.E., and Welsh M.J. Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells. Nature 347 (1990) 358-363
    • (1990) Nature , vol.347 , pp. 358-363
    • Rich, D.P.1    Anderson, M.P.2    Gregory, R.J.3    Cheng, S.H.4    Paul, S.5    Jefferson, D.M.6    McCann, J.D.7    Klinger, K.W.8    Smith, A.E.9    Welsh, M.J.10
  • 7
    • 0026641782 scopus 로고
    • The spectrum of cystic fibrosis mutations
    • Tsui L.C. The spectrum of cystic fibrosis mutations. Trends Genet. 8 (1992) 392-398
    • (1992) Trends Genet. , vol.8 , pp. 392-398
    • Tsui, L.C.1
  • 8
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • Welsh M.J., and Smith A.E. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73 (1993) 1251-1254
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 9
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng S.H., Gregory R.J., Marshall J., Paul S., Souza D.W., White G.A., O'Riordan C.R., and Smith A.E. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63 (1990) 827-834
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 10
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward C.L., and Kopito R.R. Intracellular turnover of cystic fibrosis transmembrane conductance regulator inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269 (1994) 25710-25718
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 11
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning G.M., Anderson M.P., Amara J.F., Marshall J., Smith A.E., and Welsh M.J. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358 (1992) 761-764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 12
    • 0031425079 scopus 로고    scopus 로고
    • Strategies for correcting the delta F508 CFTR protein-folding defect
    • Brown C.R., Hong-Brown L.Q., and Welch W.J. Strategies for correcting the delta F508 CFTR protein-folding defect. J. Bioenerg. Biomembr. 29 (1997) 491-502
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 491-502
    • Brown, C.R.1    Hong-Brown, L.Q.2    Welch, W.J.3
  • 13
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito R.R. Biosynthesis and degradation of CFTR. Physiol. Rev. 79 (1999) S167-S173
    • (1999) Physiol. Rev. , vol.79
    • Kopito, R.R.1
  • 14
    • 33646578825 scopus 로고    scopus 로고
    • Rescue of folding defects in ABC transporters using pharmacological chaperones
    • Loo T.W., Bartlett M.C., and Clarke D.M. Rescue of folding defects in ABC transporters using pharmacological chaperones. J. Bioenerg. Biomembr. 37 (2005) 501-507
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 501-507
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 15
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • Brown C.R., Hong-Brown L.Q., Biwersi J., Verkman A.S., and Welch W.J. Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1 (1996) 117-125
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 16
    • 24344438880 scopus 로고    scopus 로고
    • Pharmacological induction of CFTR function in patients with cystic fibrosis: mutation-specific therapy
    • Kerem E. Pharmacological induction of CFTR function in patients with cystic fibrosis: mutation-specific therapy. Pediatric Pulmonol. 40 (2005) 183-196
    • (2005) Pediatric Pulmonol. , vol.40 , pp. 183-196
    • Kerem, E.1
  • 17
    • 34548154971 scopus 로고    scopus 로고
    • Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants
    • Wang Y., Loo T.W., Bartlett M.C., and Clarke D.M. Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants. Biochem. J. 406 (2007) 257-263
    • (2007) Biochem. J. , vol.406 , pp. 257-263
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 18
    • 0037718525 scopus 로고    scopus 로고
    • ER export: call 14-3-3
    • Nufer O., and Hauri H.P. ER export: call 14-3-3. Curr. Biol. 13 (2003) R391-R393
    • (2003) Curr. Biol. , vol.13
    • Nufer, O.1    Hauri, H.P.2
  • 19
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen K., Yuan H., and Schwappach B. Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep. 6 (2005) 717-722
    • (2005) EMBO Rep. , vol.6 , pp. 717-722
    • Michelsen, K.1    Yuan, H.2    Schwappach, B.3
  • 20
    • 33745240417 scopus 로고    scopus 로고
    • F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive
    • Hegedus T., Aleksandrov A., Cui L., Gentzsch M., Chang X.B., and Riordan J.R. F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive. Biochim. Biophys. Acta 1758 (2006) 565-572
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 565-572
    • Hegedus, T.1    Aleksandrov, A.2    Cui, L.3    Gentzsch, M.4    Chang, X.B.5    Riordan, J.R.6
  • 21
    • 0033166350 scopus 로고    scopus 로고
    • Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis
    • Chang X.B., Cui L., Hou Y.X., Jensen T.J., Aleksandrov A.A., Mengos A., and Riordan J.R. Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis. Mol. Cell 4 (1999) 137-142
    • (1999) Mol. Cell , vol.4 , pp. 137-142
    • Chang, X.B.1    Cui, L.2    Hou, Y.X.3    Jensen, T.J.4    Aleksandrov, A.A.5    Mengos, A.6    Riordan, J.R.7
  • 22
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast
    • Teem J.L., Berger H.A., Ostedgaard L.S., Rich D.P., Tsui L.C., and Welsh M.J. Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast. Cell 73 (1993) 335-346
    • (1993) Cell , vol.73 , pp. 335-346
    • Teem, J.L.1    Berger, H.A.2    Ostedgaard, L.S.3    Rich, D.P.4    Tsui, L.C.5    Welsh, M.J.6
  • 23
    • 0037184104 scopus 로고    scopus 로고
    • Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508
    • DeCarvalho A.C., Gansheroff L.J., and Teem J.L. Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508. J. Biol. Chem. 277 (2002) 35896-35905
    • (2002) J. Biol. Chem. , vol.277 , pp. 35896-35905
    • DeCarvalho, A.C.1    Gansheroff, L.J.2    Teem, J.L.3
  • 24
    • 33845197320 scopus 로고    scopus 로고
    • Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms
    • Roxo-Rosa M., Xu Z., Schmidt A., Neto M., Cai Z., Soares C.M., Sheppard D.N., and Amaral M.D. Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms. Proc. Natl. Acad.Sci.U. S. A. 103 (2006) 17891-17896
    • (2006) Proc. Natl. Acad.Sci.U. S. A. , vol.103 , pp. 17891-17896
    • Roxo-Rosa, M.1    Xu, Z.2    Schmidt, A.3    Neto, M.4    Cai, Z.5    Soares, C.M.6    Sheppard, D.N.7    Amaral, M.D.8
  • 27
    • 33645698431 scopus 로고    scopus 로고
    • Proteomic analysis of nasal cells from cystic fibrosis patients and non-cystic fibrosis control individuals: search for novel biomarkers of cystic fibrosis lung disease
    • Roxo-Rosa M., da Costa G., Luider T.M., Scholte B.J., Coelho A.V., Amaral M.D., and Penque D. Proteomic analysis of nasal cells from cystic fibrosis patients and non-cystic fibrosis control individuals: search for novel biomarkers of cystic fibrosis lung disease. Proteomics 6 (2006) 2314-2325
    • (2006) Proteomics , vol.6 , pp. 2314-2325
    • Roxo-Rosa, M.1    da Costa, G.2    Luider, T.M.3    Scholte, B.J.4    Coelho, A.V.5    Amaral, M.D.6    Penque, D.7
  • 28
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom J., Nordhoff E., Mirgorodskaya E., Ekman R., and Roepstorff P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34 (1999) 105-116
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 33
    • 46749108883 scopus 로고    scopus 로고
    • Chemical rescue of deltaF508-CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells
    • Singh O.V., Pollard H.B., and Zeitlin P.L. Chemical rescue of deltaF508-CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells. Mol. Cell Proteomics 7 (2008) 1099-1110
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1099-1110
    • Singh, O.V.1    Pollard, H.B.2    Zeitlin, P.L.3
  • 34
    • 2342651419 scopus 로고    scopus 로고
    • Mackintosh, 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio M., Geraghty K.M., Wong B.H., Wood N.T., Campbell D.G., Morrice N., and Mackintosh C. Mackintosh, 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem. J. 379 (2004) 395-408
    • (2004) Biochem. J. , vol.379 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    Mackintosh, C.7
  • 36
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek S.E., Lane W.S., and Piwnica-Worms H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J. Biol. Chem. 279 (2004) 32046-32054
    • (2004) J. Biol. Chem. , vol.279 , pp. 32046-32054
    • Meek, S.E.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 41
    • 0034703069 scopus 로고    scopus 로고
    • E3KARP mediates the association of ezrin and protein kinase A with the cystic fibrosis transmembrane conductance regulator in airway cells
    • Sun F., Hug M.J., Lewarchik C.M., Yun C.H., Bradbury N.A., and Frizzell R.A. E3KARP mediates the association of ezrin and protein kinase A with the cystic fibrosis transmembrane conductance regulator in airway cells. J. Biol. Chem. 275 (2000) 29539-29546
    • (2000) J. Biol. Chem. , vol.275 , pp. 29539-29546
    • Sun, F.1    Hug, M.J.2    Lewarchik, C.M.3    Yun, C.H.4    Bradbury, N.A.5    Frizzell, R.A.6
  • 43
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M., and Kaufman R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74 (2005) 739-789
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 44
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • Zhang K., and Kaufman R.J. Signaling the unfolded protein response from the endoplasmic reticulum. J. Biol. Chem. 279 (2004) 25935-25938
    • (2004) J. Biol. Chem. , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2
  • 45
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken E., and Braakman I. Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. 40 (2005) 191-228
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 191-228
    • van Anken, E.1    Braakman, I.2
  • 46
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E., Logue S.E., Gorman A.M., and Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep. 7 (2006) 880-885
    • (2006) EMBO Rep. , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 47
    • 36849077205 scopus 로고    scopus 로고
    • Coupling cystic fibrosis to endoplasmic reticulum stress: differential role of Grp78 and ATF6
    • Kerbiriou M., Le Drevo M.A., Ferec C., and Trouve P. Coupling cystic fibrosis to endoplasmic reticulum stress: differential role of Grp78 and ATF6. Biochim. Biophys. Acta 1772 (2007) 1236-1249
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 1236-1249
    • Kerbiriou, M.1    Le Drevo, M.A.2    Ferec, C.3    Trouve, P.4
  • 49
    • 70449521295 scopus 로고    scopus 로고
    • Low temperature restoring effect on F508del-CFTR misprocessing: a proteomic approach
    • Gomes-Alves P., Sofia N., Coelho A.V., and Penque D. Low temperature restoring effect on F508del-CFTR misprocessing: a proteomic approach. J. Proteomics 73 2 (2009) 218-230
    • (2009) J. Proteomics , vol.73 , Issue.2 , pp. 218-230
    • Gomes-Alves, P.1    Sofia, N.2    Coelho, A.V.3    Penque, D.4
  • 50
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng E.A., Carlson L.M., Gutman D.M., Harrington Jr. W.J., Lee K.P., and Boise L.H. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107 (2006) 4907-4916
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 52
    • 16644375815 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6
    • Hong M., Li M., Mao C., and Lee A.S. Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6. J. Cell Biochem. 92 (2004) 723-732
    • (2004) J. Cell Biochem. , vol.92 , pp. 723-732
    • Hong, M.1    Li, M.2    Mao, C.3    Lee, A.S.4
  • 54
    • 35848935847 scopus 로고    scopus 로고
    • Regulation of ubiquitin-proteasome system mediated degradation by cytosolic stress
    • Kelly S.M., Vanslyke J.K., and Musil L.S. Regulation of ubiquitin-proteasome system mediated degradation by cytosolic stress. Mol. Biol. Cell 18 (2007) 4279-4291
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4279-4291
    • Kelly, S.M.1    Vanslyke, J.K.2    Musil, L.S.3
  • 55
    • 33845416970 scopus 로고    scopus 로고
    • Global organization and function of mammalian cytosolic proteasome pools: implications for PA28 and 19S regulatory complexes
    • Shibatani T., Carlson E.J., Larabee F., McCormack A.L., Früh K., and Skach W.R. Global organization and function of mammalian cytosolic proteasome pools: implications for PA28 and 19S regulatory complexes. Mol. Biol. Cell 17 (2006) 4962-4971
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4    Früh, K.5    Skach, W.R.6
  • 57
    • 0030610583 scopus 로고    scopus 로고
    • Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF
    • Yabe D., Nakamura T., Kanazawa N., Tashiro K., and Honjo T. Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF. J. Biol. Chem. 272 (1997) 18232-18239
    • (1997) J. Biol. Chem. , vol.272 , pp. 18232-18239
    • Yabe, D.1    Nakamura, T.2    Kanazawa, N.3    Tashiro, K.4    Honjo, T.5
  • 58
    • 0033978227 scopus 로고    scopus 로고
    • The CREC family, a novel family of multiple EF-hand, low-affinity Ca(2+)-binding proteins localised to the secretory pathway of mammalian cells
    • Honore B., and Vorum H. The CREC family, a novel family of multiple EF-hand, low-affinity Ca(2+)-binding proteins localised to the secretory pathway of mammalian cells. FEBS Lett. 466 (2000) 11-18
    • (2000) FEBS Lett. , vol.466 , pp. 11-18
    • Honore, B.1    Vorum, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.