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A third interferon-gamma-induced subunit exchange in the 20S proteasome

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1996

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Kraft, Regine
Kostka, Susanne
Standera, Sybille
Stohwasser, Ralf
Kloetzel, Peter-Michael

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European Journal of Immunology. 1996, 26(4), pp. 863-869. ISSN 0014-2980. eISSN 1521-4141. Available under: doi: 10.1002/eji.1830260421

Zusammenfassung

The 20S proteasome is a protease complex of functional importance for antigen processing. Two of the 14 proteasome subunits, delta and MB1, can be replaced by the major histocompatibility complex (MHC)-encoded and interferon-gamma (IFN-gamma)-inducible subunits LMP2 and LMP7, respectively. LMP2 and LMP7 alter the cleavage site specificity of the 20S proteasome and are required for the efficient generation of T cell epitopes from a number of viral proteins and for optimal MHC class I cell surface expression. We compared the 20S proteasome subunit pattern from IFN-gamma-induced and non-induced mouse fibroblasts on two-dimensional gels and identified a third subunit exchange by microsequencing: the non-MHC-encoded subunit MECL-1 is induced by IFN-gamma and replaces a sofar barely characterized beta subunit designated 'MC14'. In analogy to LMP2 and LMP7, MECL-1 may be functional in MHC class I-restricted antigen presentation.

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570 Biowissenschaften, Biologie

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ISO 690GRÖTTRUP, Marcus, Regine KRAFT, Susanne KOSTKA, Sybille STANDERA, Ralf STOHWASSER, Peter-Michael KLOETZEL, 1996. A third interferon-gamma-induced subunit exchange in the 20S proteasome. In: European Journal of Immunology. 1996, 26(4), pp. 863-869. ISSN 0014-2980. eISSN 1521-4141. Available under: doi: 10.1002/eji.1830260421
BibTex
@article{Grottrup1996-04third-22319,
  year={1996},
  doi={10.1002/eji.1830260421},
  title={A third interferon-gamma-induced subunit exchange in the 20S proteasome},
  number={4},
  volume={26},
  issn={0014-2980},
  journal={European Journal of Immunology},
  pages={863--869},
  author={Gröttrup, Marcus and Kraft, Regine and Kostka, Susanne and Standera, Sybille and Stohwasser, Ralf and Kloetzel, Peter-Michael}
}
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