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Science 26 August 1994:
Vol. 265. no. 5176, pp. 1234 - 1237
DOI: 10.1126/science.8066463
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Articles

Science, Vol 265, Issue 5176, 1234-1237
Copyright © 1994 by American Association for the Advancement of Science

articles

MHC class I expression in mice lacking the proteasome subunit LMP-7

HJ Fehling, W Swat, C Laplace, R Kuhn, K Rajewsky, U Muller, and H von Boehmer

Basel Institute for Immunology, Switzerland.

Proteasomes degrade endogenous proteins. Two subunits, LMP-2 and LMP-7, are encoded in a region of the major histocompatibility complex (MHC) that is critical for class I-restricted antigen presentation. Mice with a targeted deletion of the gene encoding LMP-7 have reduced levels of MHC class I cell-surface expression and present the endogenous antigen HY inefficiently; addition of peptides to splenocytes deficient in LMP-7 restores wild-type class I expression levels. This demonstrates the involvement of LMP-7 in the MHC class I presentation pathway and suggests that LMP-7 functions as an integral part of the peptide supply machinery.


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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
Allelic Differences in the Relationship Between Proteasome Activity and MHC Class I Peptide Loading.
A. M. Benham, M. Gromme, and J. Neefjes (1998)
J. Immunol. 161, 83-89
   Abstract »    Full Text »    PDF »
Proteasomes Can Either Generate or Destroy MHC Class I Epitopes: Evidence for Nonproteasomal Epitope Generation in the Cytosol.
C. J. Luckey, G. M. King, J. A. Marto, S. Venketeswaran, B. F. Maier, V. L. Crotzer, T. A. Colella, J. Shabanowitz, D. F. Hunt, and V. H. Engelhard (1998)
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   Abstract »    Full Text »    PDF »
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W. Heinemeyer, M. Fischer, T. Krimmer, U. Stachon, and D. H. Wolf (1997)
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Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide.
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The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome.
M. Groettrup, S. Standera, R. Stohwasser, and P. M. Kloetzel (1997)
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The Listeria monocytogenes-secreted p60 Protein Is an N-end Rule Substrate in the Cytosol of Infected Cells. IMPLICATIONS FOR MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I ANTIGEN PROCESSING OF BACTERIAL PROTEINS.
A. J. A. M. Sijts, I. Pilip, and E. G. Pamer (1997)
J. Biol. Chem. 272, 19261-19268
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The LMP2 polymorphism is associated with susceptibility to acute anterior uveitis in HLA-B27 positive juvenile and adult Mexican subjects with ankylosing spondylitis.
W. P Maksymowych, G. S Jhangri, C. Gorodezky, M. Luong, C. Wong, R. Burgos-Vargas, M. Morenot, J. Sanchez-Corona, C. Ramos-Remus, and A. S Russell (1997)
Ann Rheum Dis 56, 488-492
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Potential Immunocompetence of Proteolytic Fragments Produced by Proteasomes before Evolution of the Vertebrate Immune System.
G. Niedermann, R. Grimm, E. Geier, M. Maurer, C. Realini, C. Gartmann, J. Soll, S. Omura, M. C. Rechsteiner, W. Baumeister, et al. (1997)
J. Exp. Med. 186, 209-220
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Interferon-gamma Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells.
W. Ma, P. J. Lehner, P. Cresswell, J. S. Pober, and D. R. Johnson (1997)
J. Biol. Chem. 272, 16585-16590
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A. Craiu, M. Gaczynska, T. Akopian, C. F. Gramm, G. Fenteany, A. L. Goldberg, and K. L. Rock (1997)
J. Biol. Chem. 272, 13437-13445
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A Proteasome Cap Subunit Required for Spindle Pole Body Duplication in Yeast.
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Proteasome Subunits X and Y Alter Peptidase Activities in Opposite Ways to the Interferon-gamma -induced Subunits LMP2 and LMP7.
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Purification and Characterization of the Heat Shock Proteins HslV and HslU That Form a New ATP-dependent Protease in Escherichia coli.
S. J. Yoo, J. H. Seol, D. H. Shin, M. Rohrwild, M.-S. Kang, K. Tanaka, A. L. Goldberg, and C. H. Chung (1996)
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