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Volumn 1783, Issue 9, 2008, Pages 1585-1594

Role of calnexin in the ER quality control and productive folding of CFTR; differential effect of calnexin knockout on wild-type and ΔF508 CFTR

Author keywords

Calnexin; Calnexin knockout; CFTR; ER quality control

Indexed keywords

CALNEXIN; CHLORIDE CHANNEL; PROTEASOME; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 49149090813     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.04.002     Document Type: Article
Times cited : (28)

References (52)
  • 4
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bear C.E., Li C.H., Kartner N., Bridges R.J., Jensen T.J., Ramjeesingh M., and Riordan J.R. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR). Cell 68 (1992) 809-818
    • (1992) Cell , vol.68 , pp. 809-818
    • Bear, C.E.1    Li, C.H.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5    Ramjeesingh, M.6    Riordan, J.R.7
  • 8
    • 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
  • 9
    • 0036258208 scopus 로고    scopus 로고
    • Cystic fibrosis: a worldwide analysis of CFTR mutations-correlation with incidence data and application to screening
    • Bobadilla J.L., Macek Jr. M., Fine J.P., and Farrell P.M. Cystic fibrosis: a worldwide analysis of CFTR mutations-correlation with incidence data and application to screening. Hum. Mutat. 19 (2002) 575-606
    • (2002) Hum. Mutat. , vol.19 , pp. 575-606
    • Bobadilla, J.L.1    Macek Jr., M.2    Fine, J.P.3    Farrell, P.M.4
  • 10
    • 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
  • 11
    • 0027483610 scopus 로고
    • The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR
    • Li C., Ramjeesingh M., Reyes E., Jensen T., Chang X., Rommens J.M., and Bear C.E. The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR. Nat. Genet. 3 (1993) 311-316
    • (1993) Nat. Genet. , vol.3 , pp. 311-316
    • Li, C.1    Ramjeesingh, M.2    Reyes, E.3    Jensen, T.4    Chang, X.5    Rommens, J.M.6    Bear, C.E.7
  • 12
    • 0028928021 scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
    • Knittler M.R., Dirks S., and Haas I.G. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 1764-1768
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 13
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., and Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83 (1995) 129-135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 14
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston J.A., Ward C.L., and Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J. Cell. Biol. 143 (1998) 1883-1898
    • (1998) J. Cell. Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 15
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham G.C., Patterson C., Zhang W., Younger J.M., and Cyr D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol. 3 (2001) 100-105
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 16
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman M.S., Kannegaard E.S., and Kopito R.R. A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277 (2002) 11709-11714
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 17
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • Younger J.M., Ren H.Y., Chen L., Fan C.Y., Fields A., Patterson C., and Cyr D.M. A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J. Cell. Biol. 167 (2004) 1075-1085
    • (2004) J. Cell. Biol. , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 18
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger J.M., Chen L., Ren H.Y., Rosser M.F., Turnbull E.L., Fan C.Y., Patterson C., and Cyr D.M. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126 (2006) 571-582
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6    Patterson, C.7    Cyr, D.M.8
  • 19
    • 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
  • 20
    • 5444220240 scopus 로고    scopus 로고
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
    • Wang X., Matteson J., An Y., Moyer B., Yoo J.S., Bannykh S., Wilson I.A., Riordan J.R., and Balch W.E. COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. J. Cell. Biol. 167 (2004) 65-74
    • (2004) J. Cell. Biol. , vol.167 , pp. 65-74
    • Wang, X.1    Matteson, J.2    An, Y.3    Moyer, B.4    Yoo, J.S.5    Bannykh, S.6    Wilson, I.A.7    Riordan, J.R.8    Balch, W.E.9
  • 21
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du K., Sharma M., and Lukacs G.L. The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat. Struct. Mol. Biol. 12 (2005) 17-25
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 22
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang Y., Janich S., Cohn J.A., and Wilson J.M. The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9480-9484
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 23
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind S., Riordan J.R., and Williams D.B. Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269 (1994) 12784-12788
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 25
    • 34547760398 scopus 로고    scopus 로고
    • Improved maturation of CFTR by an ER export signal
    • Wendeler M.W., Nufer O., and Hauri H.P. Improved maturation of CFTR by an ER export signal. Faseb. J. 21 (2007) 2352-2358
    • (2007) Faseb. J. , vol.21 , pp. 2352-2358
    • Wendeler, M.W.1    Nufer, O.2    Hauri, H.P.3
  • 26
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo M.A., Jensen T.J., Cui L., Hou Y., Chang X.B., and Riordan J.R. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. Embo. J. 17 (1998) 6879-6887
    • (1998) Embo. J. , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 27
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham G.C., Lu Z., King S., Sorscher E., Tousson A., and Cyr D.M. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. Embo. J. 18 (1999) 1492-1505
    • (1999) Embo. J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 28
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • Alberti S., Bohse K., Arndt V., Schmitz A., and Hohfeld J. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol. Biol. Cell. 15 (2004) 4003-4010
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 30
    • 20344378216 scopus 로고    scopus 로고
    • Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin
    • Farinha C.M., and Amaral M.D. Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin. Mol. Cell. Biol. 25 (2005) 5242-5252
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5242-5252
    • Farinha, C.M.1    Amaral, M.D.2
  • 33
    • 33645211759 scopus 로고    scopus 로고
    • Rescue of functional delF508-CFTR channels in cystic fibrosis epithelial cells by the alpha-glucosidase inhibitor miglustat
    • Norez C., Noel S., Wilke M., Bijvelds M., Jorna H., Melin P., DeJonge H., and Becq F. Rescue of functional delF508-CFTR channels in cystic fibrosis epithelial cells by the alpha-glucosidase inhibitor miglustat. FEBS. Lett. 580 (2006) 2081-2086
    • (2006) FEBS. Lett. , vol.580 , pp. 2081-2086
    • Norez, C.1    Noel, S.2    Wilke, M.3    Bijvelds, M.4    Jorna, H.5    Melin, P.6    DeJonge, H.7    Becq, F.8
  • 35
    • 11244275511 scopus 로고    scopus 로고
    • Novel adenoviral vectors coding for GFP-tagged wtCFTR and deltaF508-CFTR: characterization of expression and electrophysiological properties in A549 cells
    • Vais H., Gao G.P., Yang M., Tran P., Louboutin J.P., Somanathan S., Wilson J.M., and Reenstra W.W. Novel adenoviral vectors coding for GFP-tagged wtCFTR and deltaF508-CFTR: characterization of expression and electrophysiological properties in A549 cells. Pflugers. Arch. 449 (2004) 278-287
    • (2004) Pflugers. Arch. , vol.449 , pp. 278-287
    • Vais, H.1    Gao, G.P.2    Yang, M.3    Tran, P.4    Louboutin, J.P.5    Somanathan, S.6    Wilson, J.M.7    Reenstra, W.W.8
  • 38
    • 0037192856 scopus 로고    scopus 로고
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway
    • Yoo J.S., Moyer B.D., Bannykh S., Yoo H.M., Riordan J.R., and Balch W.E. Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway. J. Biol. Chem. 277 (2002) 11401-11409
    • (2002) J. Biol. Chem. , vol.277 , pp. 11401-11409
    • Yoo, J.S.1    Moyer, B.D.2    Bannykh, S.3    Yoo, H.M.4    Riordan, J.R.5    Balch, W.E.6
  • 40
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs G.L., Mohamed A., Kartner N., Chang X.B., Riordan J.R., and Grinstein S. Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. Embo. J. 13 (1994) 6076-6086
    • (1994) Embo. J. , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1    Mohamed, A.2    Kartner, N.3    Chang, X.B.4    Riordan, J.R.5    Grinstein, S.6
  • 41
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., and Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995) 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 42
  • 43
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A., and Aebi M. Intracellular functions of N-linked glycans. Science 291 (2001) 2364-2369
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 44
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: from the ER lumen to the extracellular space
    • Johnson S., Michalak M., Opas M., and Eggleton P. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell. Biol. 11 (2001) 122-129
    • (2001) Trends Cell. Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 45
    • 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. Annu. Rev. Biochem. 73 (2004) 1019-1049
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 46
    • 0028076031 scopus 로고
    • Folding of VSV G protein: sequential interaction with BiP and calnexin
    • Hammond C., and Helenius A. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266 (1994) 456-458
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 48
    • 27944464985 scopus 로고    scopus 로고
    • Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence
    • Molinari M., Galli C., Vanoni O., Arnold S.M., and Kaufman R.J. Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol. Cell. 20 (2005) 503-512
    • (2005) Mol. Cell. , vol.20 , pp. 503-512
    • Molinari, M.1    Galli, C.2    Vanoni, O.3    Arnold, S.M.4    Kaufman, R.J.5
  • 49
    • 0028221225 scopus 로고
    • Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum
    • Rajagopalan S., and Brenner M.B. Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum. J. Exp. Med. 180 (1994) 407-412
    • (1994) J. Exp. Med. , vol.180 , pp. 407-412
    • Rajagopalan, S.1    Brenner, M.B.2
  • 50
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S., Xu Y., and Brenner M.B. Retention of unassembled components of integral membrane proteins by calnexin. Science 263 (1994) 387-390
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 51
    • 1542305433 scopus 로고    scopus 로고
    • Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
    • Leach M.R., and Williams D.B. Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation. J. Biol. Chem. 279 (2004) 9072-9079
    • (2004) J. Biol. Chem. , vol.279 , pp. 9072-9079
    • Leach, M.R.1    Williams, D.B.2


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