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Adenovirus E1A interacts directly with, and regulates the level of expression of, the immunoproteasome component MECL1.

Berhane, S, Aresté, C, Ablack, JN, Ryan, GB, Blackbourn, DJ, Mymryk, JS, Turnell, AS, Steele, JC and Grand, RJ (2011) Adenovirus E1A interacts directly with, and regulates the level of expression of, the immunoproteasome component MECL1. Virology, 421 (2). pp. 149-158.

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Abstract

Proteasomes represent the major non-lysosomal mechanism responsible for the degradation of proteins. Following interferon γ treatment 3 proteasome subunits are replaced producing immunoproteasomes. Adenovirus E1A interacts with components of the 20S and 26S proteasome and can affect presentation of peptides. In light of these observations we investigated the relationship of AdE1A to the immunoproteasome. AdE1A interacts with the immunoproteasome subunit, MECL1. In contrast, AdE1A binds poorly to the proteasome β2 subunit which is replaced by MECL1 in the conversion of proteasomes to immunoproteasomes. Binding sites on E1A for MECL1 correspond to the N-terminal region and conserved region 3. Furthermore, AdE1A causes down-regulation of MECL1 expression, as well as LMP2 and LMP7, induced by interferon γ treatment during Ad infections or following transient transfection. Consistent with previous reports AdE1A reduced IFNγ-stimulated STAT1 phosphorylation which appeared to be responsible for its ability to reduce expression of immunoproteasome subunits.

Item Type: Article
Authors :
NameEmailORCID
Berhane, SUNSPECIFIEDUNSPECIFIED
Aresté, CUNSPECIFIEDUNSPECIFIED
Ablack, JNUNSPECIFIEDUNSPECIFIED
Ryan, GBUNSPECIFIEDUNSPECIFIED
Blackbourn, DJd.blackbourn@surrey.ac.ukUNSPECIFIED
Mymryk, JSUNSPECIFIEDUNSPECIFIED
Turnell, ASUNSPECIFIEDUNSPECIFIED
Steele, JCUNSPECIFIEDUNSPECIFIED
Grand, RJUNSPECIFIEDUNSPECIFIED
Date : 20 December 2011
Identification Number : https://doi.org/10.1016/j.virol.2011.09.025
Uncontrolled Keywords : Adenoviridae, Adenovirus E1A Proteins, Binding Sites, Cell Line, Tumor, Cysteine Endopeptidases, Down-Regulation, Humans, Interferon-gamma, Phosphorylation, Proteasome Endopeptidase Complex, Protein Binding, STAT1 Transcription Factor, Signal Transduction
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 09:51
Last Modified : 17 May 2017 14:45
URI: http://epubs.surrey.ac.uk/id/eprint/825381

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