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Transient aggregation of ubiquitinated proteins during dendritic cell maturation

Transient aggregation of ubiquitinated proteins during dendritic cell maturation Dendritic cells (DCs) are antigen-presenting cells with the unique capacity to initiate primary immune responses 1 . Dendritic cells have a remarkable pattern of differentiation (maturation) that exhibits highly specific mechanisms to control antigen presentation restricted by major histocompatibility complex (MHC) 2 . MHC class I molecules present to CD8+ cytotoxic T cells peptides that are derived mostly from cytosolic proteins, which are ubiquitinated and then degraded by the proteasome 3,4 . Here we show that on inflammatory stimulation, DCs accumulate newly synthesized ubiquitinated proteins in large cytosolic structures. These structures are similar to, but distinct from, aggresomes and inclusion bodies observed in many amyloid diseases 5,6 . Notably, these dendritic cell aggresome-like induced structures (DALIS) are transient, require continuous protein synthesis and do not affect the ubiquitin–proteasome pathway. Our observations suggest the existence of an organized prioritization of protein degradation in stimulated DCs, which is probably important for regulating MHC class I presentation during maturation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Transient aggregation of ubiquitinated proteins during dendritic cell maturation

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References (30)

Publisher
Springer Journals
Copyright
Copyright © 2002 by Macmillan Magazines Ltd.
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/417177a
Publisher site
See Article on Publisher Site

Abstract

Dendritic cells (DCs) are antigen-presenting cells with the unique capacity to initiate primary immune responses 1 . Dendritic cells have a remarkable pattern of differentiation (maturation) that exhibits highly specific mechanisms to control antigen presentation restricted by major histocompatibility complex (MHC) 2 . MHC class I molecules present to CD8+ cytotoxic T cells peptides that are derived mostly from cytosolic proteins, which are ubiquitinated and then degraded by the proteasome 3,4 . Here we show that on inflammatory stimulation, DCs accumulate newly synthesized ubiquitinated proteins in large cytosolic structures. These structures are similar to, but distinct from, aggresomes and inclusion bodies observed in many amyloid diseases 5,6 . Notably, these dendritic cell aggresome-like induced structures (DALIS) are transient, require continuous protein synthesis and do not affect the ubiquitin–proteasome pathway. Our observations suggest the existence of an organized prioritization of protein degradation in stimulated DCs, which is probably important for regulating MHC class I presentation during maturation.

Journal

Nature – Springer Journals

Published: May 9, 2002

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