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Volumn 287, Issue 21, 2012, Pages 17801-17811

Erratum: Withdrawal: The role of ERp44 in maturation of serotonin transporter protein(Journal of Biological Chemistry(2019) 294(70) DOI:10.1074/jbc.M112.345058);The role of ERp44 in maturation of serotonin transporter protein

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM COMPOUNDS; BIOCHEMISTRY; CELL MEMBRANES; COENZYMES; COVALENT BONDS; OLIGOMERS; SULFUR COMPOUNDS;

EID: 84861215847     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.W118.007073     Document Type: Erratum
Times cited : (20)

References (37)
  • 1
    • 0027240164 scopus 로고
    • Neurotransmitter transporters: Three distinct gene families
    • DOI 10.1016/0959-4388(93)90126-J
    • Amara, S. G., and Arriza, J. L. (1993) Neurotransmitter transporters: Three distinct gene families. Curr. Opin. Neurobiol. 3, 337-344 (Pubitemid 23210943)
    • (1993) Current Opinion in Neurobiology , vol.3 , Issue.3 , pp. 337-344
    • Amara, S.G.1    Arriza, J.L.2
  • 2
    • 0027364736 scopus 로고
    • From synapse to vesicle: The reuptake and storage of biogenic amine neurotransmitters
    • DOI 10.1016/0005-2728(93)90109-S
    • Rudnick, G., and Clark, J. (1993) From synapse to vesicle. The re-uptake and storage of biogenic amine neurotransmitters. Biochim. Biophys. Acta 1144, 249-263 (Pubitemid 23290252)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1144 , Issue.3 , pp. 249-263
    • Rudnick, G.1    Clark, J.2
  • 4
    • 0028950155 scopus 로고
    • Identification and characterization of antidepressant-sensitive serotonin transporter proteins using site-specific antibodies
    • Qian, Y., Melikian, H. E., Rye, D. B., Levey, A. I., Blakely, R. D. (1995) Identification and characterization of antidepressant-sensitive serotonin transporter proteins using site-specific antibodies. J. Neurosci. 15, 1261-1274
    • (1995) J. Neurosci. , vol.15 , pp. 1261-1274
    • Qian, Y.1    Melikian, H.E.2    Rye, D.B.3    Levey, A.I.4    Blakely, R.D.5
  • 6
    • 0037462827 scopus 로고    scopus 로고
    • Oligomerization and trafficking of the human dopamine transporter: Mutational analysis identifies critical domains important for the functional expression of the transporter
    • DOI 10.1074/jbc.M201926200
    • Torres, G. E., Carneiro, A., Seamans, K., Fiorentini, C., Sweeney, A., Yao, W. D., Caron, M. G. (2003) Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter. J. Biol. Chem. 278, 2731-2739 (Pubitemid 36801354)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2731-2739
    • Torres, G.E.1    Carneiro, A.2    Seamans, K.3    Fiorentini, C.4    Sweeney, A.5    Yao, W.-D.6    Caron, M.G.7
  • 7
    • 0037795732 scopus 로고    scopus 로고
    • Functional consequences of homo- but not hetero-oligomerization between transporters for the biogenic amine neurotransmitters
    • DOI 10.1046/j.1471-4159.2003.01793.x
    • Kocabas, A. M., Rudnick, G., and Kilic, F. (2003) Functional consequences of homo- but not hetero-oligomerization between transporters for the biogenic amine neurotransmitters. J. Neurochem. 85, 1513-1520 (Pubitemid 36702563)
    • (2003) Journal of Neurochemistry , vol.85 , Issue.6 , pp. 1513-1520
    • Kocabas, A.M.1    Rudnick, G.2    Kilic, F.3
  • 8
    • 0030038568 scopus 로고    scopus 로고
    • N-linked oligosaccharides are required for cell surface expression of the norepinephrine transporter but do not influence substrate or inhibitor recognition
    • Nguyen, T. T., and Amara, S. G. (1996) N-Linked oligosaccharides are required for cell surface expression of the norepinephrine transporter but do not influence substrate or inhibitor recognition. J. Neurochem. 67, 645-655 (Pubitemid 26255660)
    • (1996) Journal of Neurochemistry , vol.67 , Issue.2 , pp. 645-655
    • Nguyen, T.T.1    Amara, S.G.2
  • 9
    • 0027960964 scopus 로고
    • --dependent serotonin transporter expressed using recombinant baculovirus in insect cells
    • --dependent serotonin transporter expressed using recombinant baculovirus in insect cells. J. Biol. Chem. 269, 26303-26310
    • (1994) J. Biol. Chem. , vol.269 , pp. 26303-26310
    • Tate, C.G.1    Blakely, R.D.2
  • 10
    • 0242415188 scopus 로고    scopus 로고
    • Glycosyl modification facilitates homo- and hetero-oligomerization of the serotonin transporter. A specific role for sialic acid residues
    • DOI 10.1074/jbc.M306360200
    • Ozaslan, D., Wang, S., Ahmed, B. A., Kocabas, A. M., McCastlain, J. C., Bene, A., and Kilic, F. (2003) Glycosyl modification facilitates homo- and hetero-oligomerization of serotonin transporter. A specific role for sialic acid residues. J. Biol. Chem. 278, 43991-44000 (Pubitemid 37377138)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 43991-44000
    • Ozaslan, D.1    Wang, S.2    Ahmed, B.A.3    Kocabas, A.M.4    McCastlain, J.C.5    Bene, A.6    Kilic, F.7
  • 11
    • 0031033676 scopus 로고    scopus 로고
    • External cysteine residues in the serotonin transporter
    • Chen, J. G., Lui-Chen, S., and Rudnick, G. (1997) External cysteine residues in the serotonin transporter. Biochemistry 36, 1479-1486
    • (1997) Biochemistry , vol.36 , pp. 1479-1486
    • Chen, J.G.1    Lui-Chen, S.2    Rudnick, G.3
  • 12
    • 34247276092 scopus 로고    scopus 로고
    • Direct evidence that two cysteines in the dopamine transporter form a disulfide bond
    • DOI 10.1007/s11010-006-9348-7
    • Chen, R., Wei, H., Hill, E. R., Chen, L., Jiang, L., Han, D. D., Gu, H. H. (2007) Direct evidence that two cysteines in the dopamine transporter form a disulfide bond. Mol. Cell Biochem. 298, 41-48 (Pubitemid 46605282)
    • (2007) Molecular and Cellular Biochemistry , vol.298 , Issue.1-2 , pp. 41-48
    • Chen, R.1    Wei, H.2    Hill, E.R.3    Chen, L.4    Jiang, L.5    Han, D.D.6    Gu, H.H.7
  • 13
    • 54349088443 scopus 로고    scopus 로고
    • Characterization of the endogenous human peripheral serotonin transporter SLC6A4 reveals surface expression without N-glycosylation
    • Chamba, A., Holder, M. J., Barnes, N. M., Gordon, J. (2008) Characterization of the endogenous human peripheral serotonin transporter SLC6A4 reveals surface expression without N-glycosylation. J. Neuroimmunol. 204, 75-84
    • (2008) J. Neuroimmunol. , vol.204 , pp. 75-84
    • Chamba, A.1    Holder, M.J.2    Barnes, N.M.3    Gordon, J.4
  • 14
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding, and aggregation
    • Dobson, C. M. (2004) Principles of protein folding, misfolding, and aggregation. Semin. Cell Dev. Biol. 15, 3-16
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 15
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • DOI 10.1038/sj.emboj.7601974, PII 7601974
    • Anelli, T., and Sitia, R. (2008) Protein quality control in the early secretory pathway. EMBO J. 27, 315-327 (Pubitemid 351161662)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 16
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • DOI 10.1016/j.ceb.2004.06.012, PII S095506740400081X
    • Kleizen, B., and Braakman, I. (2004) Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16, 343-349 (Pubitemid 38903139)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 17
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • DOI 10.1038/nature02262
    • Sitia, R., and Braakman, I. (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426, 891-894 (Pubitemid 38056881)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 18
    • 0022841072 scopus 로고
    • Anion-exchange and glucose transport proteins. Structure, function, and distribution
    • Lodish, H. F. (1986) Anion-exchange and glucose transport proteins. Structure, function, and distribution. Harvey Lect. 82, 19-46
    • (1986) Harvey Lect. , vol.82 , pp. 19-46
    • Lodish, H.F.1
  • 19
    • 0030593725 scopus 로고    scopus 로고
    • Membrane fusion. Timing is everything
    • Aridor, M., and Balch, W. E. (1996) Membrane fusion. Timing is everything. Nature 383, 220-221
    • (1996) Nature , vol.383 , pp. 220-221
    • Aridor, M.1    Balch, W.E.2
  • 20
    • 0021280849 scopus 로고
    • Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex
    • Lodish, H. F., Kong, N. (1984) Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell Biol. 98, 1720-1729 (Pubitemid 14102598)
    • (1984) Journal of Cell Biology , vol.98 , Issue.5 , pp. 1720-1729
    • Lodish, H.F.1    Kong, N.2
  • 21
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 22
    • 0031017637 scopus 로고    scopus 로고
    • An extracellular loop region of the serotonin transporter may be involved in the translocation mechanism
    • Stephan, M. M., Chen, M. A., Penado, K. M., Rudnick, G. (1997) An extracellular loop region of the serotonin transporter may be involved in the translocation mechanism. Biochemistry 36, 1322-1328
    • (1997) Biochemistry , vol.36 , pp. 1322-1328
    • Stephan, M.M.1    Chen, M.A.2    Penado, K.M.3    Rudnick, G.4
  • 23
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • DOI 10.1038/nrm1052
    • Ellgaard, L., and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191 (Pubitemid 36288040)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 24
    • 0035675962 scopus 로고    scopus 로고
    • The action of molecular chaperones in the early secretory pathway
    • DOI 10.1146/annurev.genet.35.102401.090313
    • Fewell, S. W., Travers, K. J., Weissman, J. S., and Brodsky, J. L. (2001) The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet. 35, 149-191 (Pubitemid 34032974)
    • (2001) Annual Review of Genetics , vol.35 , pp. 149-191
    • Fewell, S.W.1    Travers, K.J.2    Weissman, J.S.3    Brodsky, J.L.4
  • 25
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards. Quality control in the secretory pathway
    • Ellgaard, L., Molinari, M., and Helenius, A. (1999) Setting the standards. Quality control in the secretory pathway. Science 286, 1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 27
    • 34948899397 scopus 로고    scopus 로고
    • Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis
    • DOI 10.1038/sj.emboj.7601844, PII 7601844
    • Anelli, T., Ceppi, S., Bergamelli, L., Cortini, M., Masciarelli, S., Valetti, C., Sitia, R. (2007) Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis. EMBO J. 26, 4177-4188 (Pubitemid 47525157)
    • (2007) EMBO Journal , vol.26 , Issue.19 , pp. 4177-4188
    • Anelli, T.1    Ceppi, S.2    Bergamelli, L.3    Cortini, M.4    Masciarelli, S.5    Valetti, C.6    Sitia, R.7
  • 28
    • 0029944851 scopus 로고    scopus 로고
    • Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains
    • Reddy, P., Sparvoli, A., Fagioli, C., Fassina, G., and Sitia, R. (1996) Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. EMBO J. 15, 2077-2085 (Pubitemid 26141124)
    • (1996) EMBO Journal , vol.15 , Issue.9 , pp. 2077-2085
    • Reddy, P.1    Sparvoli, A.2    Fagioli, C.3    Fassina, G.4    Sitia, R.5
  • 29
    • 34347355500 scopus 로고    scopus 로고
    • Diseases originating from altered protein quality control in the endoplasmic reticulum
    • DOI 10.2174/092986707780830952
    • Otsu, M., and Sitia, R. (2007) Diseases originating from altered protein quality control in the endoplasmic reticulum. Curr. Med. Chem. 14, 1639-1652 (Pubitemid 47010153)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.15 , pp. 1639-1652
    • Otsu, M.1    Sitia, R.2
  • 30
    • 34248197560 scopus 로고    scopus 로고
    • Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention
    • DOI 10.1128/MCB.00931-06
    • Wang, Z. V., Schraw, T. D., Kim, J. Y., Khan, T., Rajala, M. W., Follenzi, A., and Scherer, P. E. (2007) Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention. Mol. Cell Biol. 27, 3716-3731 (Pubitemid 46726179)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.10 , pp. 3716-3731
    • Wang, Z.V.1    Schraw, T.D.2    Kim, J.-Y.3    Khan, T.4    Rajala, M.W.5    Follenzi, A.6    Scherer, P.E.7
  • 32
    • 44449129593 scopus 로고    scopus 로고
    • ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum
    • Mariappan, M., Radhakrishnan, K., Dierks, T., Schmidt, B., and von Figura, K. (2008) ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum. J. Biol. Chem. 283, 6375-6583
    • (2008) J. Biol. Chem. , vol.283 , pp. 6375-6583
    • Mariappan, M.1    Radhakrishnan, K.2    Dierks, T.3    Schmidt, B.4    Von Figura, K.5
  • 33
    • 0032587512 scopus 로고    scopus 로고
    • Production of large quantifies of isotopically labeled protein in Pichia pastoris by fermentation
    • DOI 10.1023/A:1008398313350
    • Wood, M. J., and Komives, E. A. (1999) Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation. J. Biomol. NMR 13, 149-159 (Pubitemid 29089225)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.2 , pp. 149-159
    • Wood, M.J.1    Komives, E.A.2
  • 34
    • 0038558136 scopus 로고    scopus 로고
    • Characterization of glycosylation sites of the epidermal growth factor receptor
    • DOI 10.1021/bi027101p
    • Zhen, Y., Caprioli, R. M., and Staros, J. V. (2003) Characterization of glycosylation sites of the epidermal growth factor receptor. Biochemistry 42, 5478-5492 (Pubitemid 36560445)
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5478-5492
    • Zhen, Y.1    Caprioli, R.M.2    Staros, J.V.3
  • 35
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • DOI 10.1093/emboj/21.4.835
    • Anelli, T., Alessio, M., Mezghrani, A., Simmen, T., Talamo, F., Bachi, A., Sitia, R. (2002) ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21, 835-844 (Pubitemid 34174063)
    • (2002) EMBO Journal , vol.21 , Issue.4 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 37
    • 62749089363 scopus 로고    scopus 로고
    • The translocation of serotonin transporter is impeded on serotonin-altered vimentin network. A mechanism by which serotonin dictates the cellular distribution of serotonin transporter
    • Ahmed, B. A., Bukhari, I. A., Jeffus, B. C., Harney, J. T., Thyparambil, S., Ziu, E., Fraer, M., Rusch, N. J., Zimniak, P., Lupashin, V., Tang, D., and Kilic, F. (2009) The translocation of serotonin transporter is impeded on serotonin-altered vimentin network. A mechanism by which serotonin dictates the cellular distribution of serotonin transporter. PLoS ONE 4, e4730
    • (2009) PLoS ONE , vol.4
    • Ahmed, B.A.1    Bukhari, I.A.2    Jeffus, B.C.3    Harney, J.T.4    Thyparambil, S.5    Ziu, E.6    Fraer, M.7    Rusch, N.J.8    Zimniak, P.9    Lupashin, V.10    Tang, D.11    Kilic, F.12


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