Transient aggregation of ubiquitinated proteins during dendritic cell maturation

Hugues Lelouard, Evelina Gatti, Fanny Cappello, Olivia Gresser, Voahirana Camosseto and Philippe Pierre ()
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Hugues Lelouard: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy
Evelina Gatti: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy
Fanny Cappello: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy
Olivia Gresser: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy
Voahirana Camosseto: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy
Philippe Pierre: Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université Med., Campus de Luminy

Nature, 2002, vol. 417, issue 6885, 177-182

Abstract: Abstract Dendritic cells (DCs) are antigen-presenting cells with the unique capacity to initiate primary immune responses1. 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 proteasome3,4. 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 diseases5,6. 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.

Date: 2002
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DOI: 10.1038/417177a

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