메뉴 건너뛰기




Volumn 8, Issue 11, 2007, Pages 1530-1542

Aggregate formation by ERp57-deficient MHC class I peptide-loading complexes

Author keywords

Endoplasmic reticulum; ERp57; FRET; MHC class I peptide loading complex; Protein aggregates; Tapasin

Indexed keywords

ALANINE; CYSTEINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEIN P57; TAPASIN; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1;

EID: 35348897862     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2007.00639.x     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 26244455510 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing and cross-presentation
    • Cresswell P, Ackerman AL, Giodini A, Peaper DR, Wearsch PA. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol Rev 2005; 207: 145-157.
    • (2005) Immunol Rev , vol.207 , pp. 145-157
    • Cresswell, P.1    Ackerman, A.L.2    Giodini, A.3    Peaper, D.R.4    Wearsch, P.A.5
  • 2
    • 0036776746 scopus 로고    scopus 로고
    • Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum
    • Momburg F, Tan P. Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol Immunol 2002; 39: 217-233.
    • (2002) Mol Immunol , vol.39 , pp. 217-233
    • Momburg, F.1    Tan, P.2
  • 3
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M, Bouvier M. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 2007; 26: 1681-1690.
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 4
    • 33846044754 scopus 로고    scopus 로고
    • Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes
    • Garbi N, Hammerling G, Tanaka S. Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. Curr Opin Immunol 2007; 19: 99-105.
    • (2007) Curr Opin Immunol , vol.19 , pp. 99-105
    • Garbi, N.1    Hammerling, G.2    Tanaka, S.3
  • 5
  • 6
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick TP, Bangia N, Peaper DR, Cresswell P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 2002; 16: 87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 7
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper DR, Wearsch PA, Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J 2005; 24: 3613-3623.
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 8
    • 4143051423 scopus 로고    scopus 로고
    • Tapasin enhances MHC class I peptide presentation according to peptide half-life
    • Howarth M, Williams A, Tolstrup AB, Elliott T. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci U S A 2004; 101: 11737-11742.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11737-11742
    • Howarth, M.1    Williams, A.2    Tolstrup, A.B.3    Elliott, T.4
  • 9
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: A cellular response to misfolded proteins. J Cell Biol 1998; 143: 1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 10
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R, Bebok Z, Sorscher EJ, Sztul ES. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J Cell Biol 1999; 146: 1239-1254.
    • (1999) J Cell Biol , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 11
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito RR, Sitia R. Aggresomes and Russell bodies. Symptoms of cellular indigestion? EMBO Rep 2000; 1: 225-231.
    • (2000) EMBO Rep , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 12
    • 0029917002 scopus 로고    scopus 로고
    • Processing and delivery of peptides presented by MHC class I molecules
    • Lehner PJ, Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Curr Opin Immunol 1996; 8: 59-67.
    • (1996) Curr Opin Immunol , vol.8 , pp. 59-67
    • Lehner, P.J.1    Cresswell, P.2
  • 13
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi N, Tanaka S, Momburg F, Hammerling GJ. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 2006; 7: 93-102.
    • (2006) Nat Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 14
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits EA, Vos JC, Gromme M, Neefjes J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature 2000; 404: 774-778.
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.A.1    Vos, J.C.2    Gromme, M.3    Neefjes, J.4
  • 15
    • 0037083359 scopus 로고    scopus 로고
    • Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites
    • Pentcheva T, Spiliotis ET, Edidin M. Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites. J Immunol 2002; 168: 1538-1541.
    • (2002) J Immunol , vol.168 , pp. 1538-1541
    • Pentcheva, T.1    Spiliotis, E.T.2    Edidin, M.3
  • 16
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 2002; 20: 87-90.
    • (2002) Nat Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 17
    • 33947355325 scopus 로고    scopus 로고
    • Single-cell quantification of molecules and rates using open-source microscope-based cytometry
    • Gordon A, Colman-Lerner A, Chin TE, Benjamin KR, Yu RC, Brent R. Single-cell quantification of molecules and rates using open-source microscope-based cytometry. Nat Methods 2007; 4: 175-181.
    • (2007) Nat Methods , vol.4 , pp. 175-181
    • Gordon, A.1    Colman-Lerner, A.2    Chin, T.E.3    Benjamin, K.R.4    Yu, R.C.5    Brent, R.6
  • 18
    • 14644408733 scopus 로고    scopus 로고
    • Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly
    • Bangia N, Cresswell P. Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly. Immunology 2005; 114: 346-353.
    • (2005) Immunology , vol.114 , pp. 346-353
    • Bangia, N.1    Cresswell, P.2
  • 19
    • 33745863455 scopus 로고    scopus 로고
    • Biogenesis of functional antigenic peptide transporter TAP requires assembly of pre-existing TAP1 with newly synthesized TAP2
    • Keusekotten K, Leonhardt RM, Ehses S, Knittler MR. Biogenesis of functional antigenic peptide transporter TAP requires assembly of pre-existing TAP1 with newly synthesized TAP2. J Biol Chem 2006; 281: 17545-17551.
    • (2006) J Biol Chem , vol.281 , pp. 17545-17551
    • Keusekotten, K.1    Leonhardt, R.M.2    Ehses, S.3    Knittler, M.R.4
  • 20
    • 0037261366 scopus 로고    scopus 로고
    • A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
    • Garbi N, Tiwari N, Momburg F, Hammerling GJ. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur J Immunol 2003; 33: 264-273.
    • (2003) Eur J Immunol , vol.33 , pp. 264-273
    • Garbi, N.1    Tiwari, N.2    Momburg, F.3    Hammerling, G.J.4
  • 21
    • 0035187739 scopus 로고    scopus 로고
    • Assembly of tapasin-associated MHC class I in the absence of the transporter associated with antigen processing (TAP)
    • Paulsson KM, Anderson PO, Chen S, Sjogren HO, Ljunggren HG, Wang P, Li S. Assembly of tapasin-associated MHC class I in the absence of the transporter associated with antigen processing (TAP). Int Immunol 2001; 13: 23-29.
    • (2001) Int Immunol , vol.13 , pp. 23-29
    • Paulsson, K.M.1    Anderson, P.O.2    Chen, S.3    Sjogren, H.O.4    Ljunggren, H.G.5    Wang, P.6    Li, S.7
  • 22
    • 33745301876 scopus 로고    scopus 로고
    • Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products
    • Qian SB, Reits E, Neefjes J, Deslich JM, Bennink JR, Yewdell JW. Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products. J Immunol 2006; 177: 227-233.
    • (2006) J Immunol , vol.177 , pp. 227-233
    • Qian, S.B.1    Reits, E.2    Neefjes, J.3    Deslich, J.M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 23
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74: 739-789.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 24
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak SJ, Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 2006; 86: 1133-1149.
    • (2006) Physiol Rev , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 25
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev 1999; 13: 1211-1233.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 26
    • 0038446405 scopus 로고    scopus 로고
    • The unfolded protein response
    • Liu CY, Kaufman RJ. The unfolded protein response. J Cell Sci 2003; 116: 1861-1862.
    • (2003) J Cell Sci , vol.116 , pp. 1861-1862
    • Liu, C.Y.1    Kaufman, R.J.2
  • 27
    • 4744344331 scopus 로고    scopus 로고
    • Cerebral ischemia and the unfolded protein response
    • DeGracia DJ, Montie HL. Cerebral ischemia and the unfolded protein response. J Neurochem 2004; 91: 1-8.
    • (2004) J Neurochem , vol.91 , pp. 1-8
    • DeGracia, D.J.1    Montie, H.L.2
  • 28
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y, Baig E, Williams DB. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 2006; 281: 14622-14631.
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 29
    • 33646594461 scopus 로고    scopus 로고
    • Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
    • Solda T, Garbi N, Hammerling GJ, Molinari M. Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J Biol Chem 2006; 281: 6219-6226.
    • (2006) J Biol Chem , vol.281 , pp. 6219-6226
    • Solda, T.1    Garbi, N.2    Hammerling, G.J.3    Molinari, M.4
  • 30
    • 0037083299 scopus 로고    scopus 로고
    • Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
    • Tan P, Kropshofer H, Mandelboim O, Bulbuc N, Hammerling GJ, Momburg F. Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading. J Immunol 2002; 168: 1950-1960.
    • (2002) J Immunol , vol.168 , pp. 1950-1960
    • Tan, P.1    Kropshofer, H.2    Mandelboim, O.3    Bulbuc, N.4    Hammerling, G.J.5    Momburg, F.6
  • 32
    • 35348880018 scopus 로고    scopus 로고
    • Biochemical and functional characterization of the tapasin/ERp57 conjugate
    • PhD Thesis, Yale University, New Haven, CT, USA
    • Peaper DR. Biochemical and functional characterization of the tapasin/ ERp57 conjugate. PhD Thesis, 2008. Yale University, New Haven, CT, USA.
    • (2008)
    • Peaper, D.R.1
  • 33
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch PA, Cresswell P. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 2007; 8: 873-881.
    • (2007) Nat Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 34
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams DB. Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 2006; 119: 615-623.
    • (2006) J Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 36
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006; 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 37
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch K. Endoplasmic reticulum-associated degradation. Annu Rev Cell Dev Biol 2005; 21: 435-456.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 435-456
    • Romisch, K.1
  • 38
    • 0033180470 scopus 로고    scopus 로고
    • Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum
    • Marguet D, Spiliotis ET, Pentcheva T, Lebowitz M, Schneck J, Edidin M. Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum. Immunity 1999; 11: 231-240.
    • (1999) Immunity , vol.11 , pp. 231-240
    • Marguet, D.1    Spiliotis, E.T.2    Pentcheva, T.3    Lebowitz, M.4    Schneck, J.5    Edidin, M.6
  • 39
    • 33646566873 scopus 로고    scopus 로고
    • Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
    • Schrodt S, Koch J, Tampe R. Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex. J Biol Chem 2006; 281: 6455-6462.
    • (2006) J Biol Chem , vol.281 , pp. 6455-6462
    • Schrodt, S.1    Koch, J.2    Tampe, R.3
  • 40
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle
    • Kagan JC, Stein MP, Pypaert M, Roy CR. Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. J Exp Med 2004; 199: 1201-1211.
    • (2004) J Exp Med , vol.199 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 41
    • 0037007230 scopus 로고    scopus 로고
    • Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules
    • Kang SJ, Cresswell P. Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules. EMBO J 2002; 21: 1650-1660.
    • (2002) EMBO J , vol.21 , pp. 1650-1660
    • Kang, S.J.1    Cresswell, P.2
  • 43
    • 35348919755 scopus 로고    scopus 로고
    • Bethesda, MD: U.S. National Institutes of Health; 1997-2006. URL Accessed on August 27
    • Rasband W. ImageJ. Bethesda, MD: U.S. National Institutes of Health; 1997-2006. URL http://rsb.info.nih.gov/ij/. Accessed on August 27, 2007.
    • (2007) Image J.
    • Rasband, W.1
  • 44
    • 35348859211 scopus 로고    scopus 로고
    • URL 2006-2007, Accessed on August 27
    • Stepensky D. FRETcalc plugin for ImageJ. URL http://rsb.info.nih.gov/ij/ plugins/fret/fret-calc.html. 2006-2007, Accessed on August 27, 2007.
    • (2007) FRETcalc Plugin for ImageJ.
    • Stepensky, D.1
  • 45
    • 34250199380 scopus 로고    scopus 로고
    • FRETcalc plugin for calculation of FRET in non-continuous intracellular compartments
    • Stepensky D. FRETcalc plugin for calculation of FRET in non-continuous intracellular compartments. Biochem Biophys Res Commun 2007; 359: 752-758.
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 752-758
    • Stepensky, D.1
  • 46
    • 0028037401 scopus 로고
    • Quantitative analysis of folylpolyglutamate synthetase gene expression in tumor tissues by polymerase chain reaction: Marked variation of expression among leukemia patients
    • Lenz H, Danenberg K, Schnieders B, Goeker E, Peters G, Garrow T, Shane B, Bertino J, Danenberg P. Quantitative analysis of folylpolyglutamate synthetase gene expression in tumor tissues by polymerase chain reaction: Marked variation of expression among leukemia patients. Oncol Res 1994; 6: 329-335.
    • (1994) Oncol Res , vol.6 , pp. 329-335
    • Lenz, H.1    Danenberg, K.2    Schnieders, B.3    Goeker, E.4    Peters, G.5    Garrow, T.6    Shane, B.7    Bertino, J.8    Danenberg, P.9
  • 47
    • 24644495622 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response
    • Chan S, Egan P. Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J 2005; 19: 1510-1512.
    • (2005) FASEB J , vol.19 , pp. 1510-1512
    • Chan, S.1    Egan, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.