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Volumn 42, Issue 1, 2005, Pages 137-141

Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome

Author keywords

Antigen presentation; Multidrug resistance; P glycoprotein; Proteasome; TAP; Transporter associated with antigen processing

Indexed keywords

GLYCOPROTEIN P; PROTEIN SUBUNIT;

EID: 5444246363     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2004.07.005     Document Type: Article
Times cited : (18)

References (32)
  • 2
    • 0026442415 scopus 로고
    • Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules
    • D. Arnold, J. Driscoll, M. Androlewicz, E. Hughes, P. Cresswell, and T. Spies Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules Nature 360 1992 171 173
    • (1992) Nature , vol.360 , pp. 171-173
    • Arnold, D.1    Driscoll, J.2    Androlewicz, M.3    Hughes, E.4    Cresswell, P.5    Spies, T.6
  • 3
    • 0035907379 scopus 로고    scopus 로고
    • Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules
    • R.J. Binder, N.E. Blachere, and P.K. Srivastava Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules J. Biol. Chem. 276 17 2001 163 171
    • (2001) J. Biol. Chem. , vol.276 , Issue.17 , pp. 163-171
    • Binder, R.J.1    Blachere, N.E.2    Srivastava, P.K.3
  • 4
    • 0034672211 scopus 로고    scopus 로고
    • Association of immunoproteasomes with the endoplasmic reticulum
    • P.M.R. Brooks, G.G. Mason, K.B. Hendil, and A.J. Rivett Association of immunoproteasomes with the endoplasmic reticulum Biochem. J. 352 2000 611 615
    • (2000) Biochem. J. , vol.352 , pp. 611-615
    • Brooks, P.M.R.1    Mason, G.G.2    Hendil, K.B.3    Rivett, A.J.4
  • 5
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • V. Cerundolo, A. Benham, V. Braud, S. Mukherjee, K. Gould, B. Macino, J. Neefjes, and A. Townsend The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells Eur. J. Immunol. 27 1997 336 341
    • (1997) Eur. J. Immunol. , vol.27 , pp. 336-341
    • Cerundolo, V.1    Benham, A.2    Braud, V.3    Mukherjee, S.4    Gould, K.5    MacIno, B.6    Neefjes, J.7    Townsend, A.8
  • 6
    • 0035192444 scopus 로고    scopus 로고
    • Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing
    • D.A.M. Chen Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing Immunol. Lett. 75 2001 143 148
    • (2001) Immunol. Lett. , vol.75 , pp. 143-148
    • Chen, D.A.M.1
  • 7
    • 0025633562 scopus 로고
    • MHC class II region encoding proteins related to the multidrug resistance family of transmembrane transporters
    • E.V. Deverson, I.R. Gow, W.J. Coadwell, J.J. Monaco, G.W. Butcher, and J.C. Howard MHC class II region encoding proteins related to the multidrug resistance family of transmembrane transporters Nature 348 1990 738 741
    • (1990) Nature , vol.348 , pp. 738-741
    • Deverson, E.V.1    Gow, I.R.2    Coadwell, W.J.3    Monaco, J.J.4    Butcher, G.W.5    Howard, J.C.6
  • 8
    • 0032476655 scopus 로고    scopus 로고
    • Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast
    • C. Enenkel, A. Lehmann, and P.M. Kloetzel Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast EMBO J. 17 1998 6144 6154
    • (1998) EMBO J. , vol.17 , pp. 6144-6154
    • Enenkel, C.1    Lehmann, A.2    Kloetzel, P.M.3
  • 9
    • 0030037846 scopus 로고    scopus 로고
    • Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-g-induced subunits LMP2 and LMP7
    • M. Gaczynska, A.L. Goldberg, K. Tanaka, K.B. Hendil, and K.L. Rock Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-g-induced subunits LMP2 and LMP7 J. Biol. Chem. 271 1996 17275 17280
    • (1996) J. Biol. Chem. , vol.271 , pp. 17275-17280
    • Gaczynska, M.1    Goldberg, A.L.2    Tanaka, K.3    Hendil, K.B.4    Rock, K.L.5
  • 10
    • 0025771623 scopus 로고
    • A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC
    • R. Glynne, S.H. Powis, S. Beck, A. Kelly, L.-A. Kerr, and J. Trowsdale A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC Nature 353 1991 357 360
    • (1991) Nature , vol.353 , pp. 357-360
    • Glynne, R.1    Powis, S.H.2    Beck, S.3    Kelly, A.4    Kerr, L.-A.5    Trowsdale, J.6
  • 11
    • 0002337352 scopus 로고
    • Interaction trap/two-hybrid system to identify interacting proteins
    • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smithe, J.A., Struhl, K. (Eds.), Wiley, New York
    • Golemis, E., Gyuris, J., Brent, R., 1994. Interaction trap/two-hybrid system to identify interacting proteins. In: Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smithe, J.A., Struhl, K. (Eds.), Current Protocols in Molecular Biology, vol. 2. Wiley, New York, pp. 13.14.1-13.14.17.
    • (1994) Current Protocols in Molecular Biology , vol.2 , pp. 13141-131417
    • Golemis, E.1    Gyuris, J.2    Brent, R.3
  • 13
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2
    • J. Gyuris, E. Golemis, H. Chertkov, and R. Brent Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2 Cell 75 1993 791 803
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 14
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • T.J. Jensen, M.A. Loo, S. Pind, D.B. Williams, A.L. Goldberg, and J.R. Riordan 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
  • 15
    • 0035886881 scopus 로고    scopus 로고
    • Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway
    • G.M.S. Lautscham, G. Taylor, T. Haigh, A. Leese, A. Rickinson, and N. Blake Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway J. Exp. Med. 194 2001 1053 1068
    • (2001) J. Exp. Med. , vol.194 , pp. 1053-1068
    • Lautscham, G.M.S.1    Taylor, G.2    Haigh, T.3    Leese, A.4    Rickinson, A.5    Blake, N.6
  • 16
    • 0037386520 scopus 로고    scopus 로고
    • TAP-independent antigen presentation on MHC class I molecules: Lessons from Epstein-Barr virus
    • G.R.A. Lautscham, and N. Blake TAP-independent antigen presentation on MHC class I molecules: lessons from Epstein-Barr virus Microbes Infect. 5 2003 291 299
    • (2003) Microbes Infect. , vol.5 , pp. 291-299
    • Lautscham, G.R.A.1    Blake, N.2
  • 19
    • 0037931318 scopus 로고    scopus 로고
    • P-glycoprotein - A novel therapeutic target for immunomodulation in clinical transplantation and autoimmunity?
    • S. Pendse, M.H. Sayegh, and M.H. Frank P-glycoprotein - a novel therapeutic target for immunomodulation in clinical transplantation and autoimmunity? Curr Drug Targets 4 2003 469 476
    • (2003) Curr Drug Targets , vol.4 , pp. 469-476
    • Pendse, S.1    Sayegh, M.H.2    Frank, M.H.3
  • 20
    • 0026585065 scopus 로고
    • Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene
    • M. Raymond, P. Gros, M. Whiteway, and D.Y. Thomas Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene Science 256 1992 232 234
    • (1992) Science , vol.256 , pp. 232-234
    • Raymond, M.1    Gros, P.2    Whiteway, M.3    Thomas, D.Y.4
  • 21
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A.L. Goldberg Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules Cell 78 1994 761 771
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 22
    • 0025357975 scopus 로고
    • Characterization of naturally occurring minor histocompatibility peptides including H-4 and H-Y
    • O.K. Rotzschke, T. Falk, H.J. Wallny, S. Faath, and H.G. Rammensee Characterization of naturally occurring minor histocompatibility peptides including H-4 and H-Y Science 249 1990 283 287
    • (1990) Science , vol.249 , pp. 283-287
    • Rotzschke, O.K.1    Falk, T.2    Wallny, H.J.3    Faath, S.4    Rammensee, H.G.5
  • 25
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single-stranded nucleic acids as a carrier
    • R.H. Schiestl, and R.D. Gietz High efficiency transformation of intact yeast cells using single-stranded nucleic acids as a carrier Curr. Genet. 16 1989 339 346
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 26
    • 0028920219 scopus 로고
    • Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores
    • F.J. Sharom, G. DiDiodato, X. Yu, and K.J.D. Ashbourne Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores J. Biol. Chem. 270 1995 10334 10341
    • (1995) J. Biol. Chem. , vol.270 , pp. 10334-10341
    • Sharom, F.J.1    Didiodato, G.2    Yu, X.3    Ashbourne, K.J.D.4
  • 27
    • 0029987548 scopus 로고    scopus 로고
    • Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport
    • F.J. Sharom, X. Yu, G. Didiodato, and J.W.K. Chu Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport Biochem. J. 320 1996 421 428
    • (1996) Biochem. J. , vol.320 , pp. 421-428
    • Sharom, F.J.1    Yu, X.2    Didiodato, G.3    Chu, J.W.K.4
  • 28
    • 0025604835 scopus 로고
    • A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway
    • T. Spies, M. Bresnahan, S. Bahram, D. Arnold, G. Blanck, E. Mellins, D. Pious, and R. DeMars A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway Nature 348 1990 744 747
    • (1990) Nature , vol.348 , pp. 744-747
    • Spies, T.1    Bresnahan, M.2    Bahram, S.3    Arnold, D.4    Blanck, G.5    Mellins, E.6    Pious, D.7    Demars, R.8
  • 29
    • 0027548728 scopus 로고
    • The transporters associated with antigen presentation
    • A. Townsend The transporters associated with antigen presentation Sem. Cell Biol. 4 1993 53 61
    • (1993) Sem. Cell Biol. , vol.4 , pp. 53-61
    • Townsend, A.1
  • 30
    • 0025688348 scopus 로고
    • Sequences encoded in the class II region of the MHC related to the ABC superfamily of transporters
    • J. Trowsdale, I. Hanson, I. Mockridge, S. Beck, A. Townsend, and A. Kelly Sequences encoded in the class II region of the MHC related to the ABC superfamily of transporters Nature 348 1990 741 744
    • (1990) Nature , vol.348 , pp. 741-744
    • Trowsdale, J.1    Hanson, I.2    Mockridge, I.3    Beck, S.4    Townsend, A.5    Kelly, A.6
  • 31
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • C.L. Ward, S. Omura, and R.R. Kopito 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
  • 32
    • 0028107066 scopus 로고
    • Presentation of viral antigens restricted by H-2Kb Db or Kd in proteasome subunit LMP2- and LMP7-deficient cells
    • X. Zhou, F. Momburg, T. Liu, U.M. Abdel Motal, M. Jondal, G.J. Hammerling, and H.G. Ljunggren Presentation of viral antigens restricted by H-2Kb Db or Kd in proteasome subunit LMP2- and LMP7-deficient cells Eur. J. Immunol. 24 1994 1863 1868
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1863-1868
    • Zhou, X.1    Momburg, F.2    Liu, T.3    Abdel Motal, U.M.4    Jondal, M.5    Hammerling, G.J.6    Ljunggren, H.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.