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Портал Begell Электронная Бибилиотека e-Книги Журналы Справочники и Сборники статей Коллекции
Critical Reviews™ in Immunology
Импакт фактор: 1.352 5-летний Импакт фактор: 3.347 SJR: 0.657 SNIP: 0.55 CiteScore™: 2.19

ISSN Печать: 1040-8401
ISSN Онлайн: 2162-6472

Выпуски:
Том 39, 2019 Том 38, 2018 Том 37, 2017 Том 36, 2016 Том 35, 2015 Том 34, 2014 Том 33, 2013 Том 32, 2012 Том 31, 2011 Том 30, 2010 Том 29, 2009 Том 28, 2008 Том 27, 2007 Том 26, 2006 Том 25, 2005 Том 24, 2004 Том 23, 2003 Том 22, 2002 Том 21, 2001 Том 20, 2000 Том 19, 1999 Том 18, 1998 Том 17, 1997 Том 16, 1996 Том 15, 1995 Том 14, 1994

Critical Reviews™ in Immunology

DOI: 10.1615/CritRevImmunol.v21.i4.30
21 pages

Structural Plasticity of the Proteasome and Its Function in Antigen Processing

Marcus Groettrup
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland
Maries van den Broek
Institute of Experimental Immunology, Department of Pathology, University Hospital Zurich, Zurich, Switzerland
Katrin Schwarz
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland
Annalisa Macagno
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland
Selina Khan
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland
Rita de Giuli
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland
Gunter Schmidtke
Research Department, Cantonal Hospital St. Gallen, St. Gallen, Switzerland

Краткое описание

The proteasome is the main provider of peptide ligands for major histocompatibility complex class I molecules. During an immune response to pathogens, the proinflammatory cytokine interferon (IFN)-g and tumor necrosis factor (TNF)-a are released, which induce the proteasome subunits LMP2, LMP7, and MECL-1. These replace the constitutively expressed active site subunits of the proteasome (delta, MB1, and Z) leading to a marked change in the cleavage preference of the proteasome and the production of T-cell epitopes. Proteasome activity is further changed by the IFN)-g–mediated induction of the proteasome regulator PA28a/b and the downregulation of PA28g. Why such an extensive exchange of proteasome active site subunits and regulators occurs is still poorly understood. In this article we discuss recent insights in the structural consequences of proteasome reorganization and their effects on epitope generation and shaping of the cytotoxic immune response. Moreover, we review the latest data on how the ubiquitin pathway targets protein antigens for peptide processing and discuss the potential of proteasome inhibitors for the modulation of antigen presentation.


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