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A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells.

Abstract：

:Crosspresentation of exogenous antigens (Ags) to CD8(+) T cells by dendritic cells generally requires their entry into the cytosol. Here we show that both soluble and phagocytosed extracellular Ags accessed the cytosol via molecular components required for endoplasmic reticulum (ER)-associated degradation (ERAD). Exogenous Pseudomonas aeruginosa Exotoxin A, which inhibits protein translocation from the ER to the cytosol, abrogated crosspresentation. Exotoxin A also prevented the transporter associated with antigen processing (TAP) inhibitor, ICP47, from entering the cytosol and blocking TAP-mediated peptide transport. In an in vitro model of retrotranslocation, the AAA ATPase p97, an enzyme critical for ERAD, was the only cytosolic cofactor required for protein export from isolated phagosomes. Functional p97 was also required for crosspresentation but not conventional presentation. Thus, crosspresentation appears to result from an adaptation of the retrotranslocation mechanisms involved in the degradation of misfolded ER proteins.

journal_name

Immunity

journal_title

Immunity

authors

Ackerman AL,Giodini A,Cresswell P

doi

10.1016/j.immuni.2006.08.017

subject

Has Abstract

pub_date

2006-10-01 00:00:00

pages

607-17

issue

4

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(06)00426-2

journal_volume

25

pub_type

杂志文章

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