Abstract:
:As a key molecule in the antiviral innate immune response, the activation of TANK-binding kinase 1 (TBK1) is under tight regulation. In this report, we identified phosphatidylserine-specific phospholipase PLA1A as a host factor that modulates the TBK1 activation. Knockdown of PLA1A expression suppressed the innate immune signaling induced by RNA viruses, while PLA1A overexpression enhanced the signaling. PLA1A functioned at the TBK1 level of the signaling pathway, as PLA1A silencing blocked TBK1, but not interferon regulatory factor 3 (IRF3) induced interferon-β (IFN-β) promoter activity. The phosphorylation and kinase activity of TBK1 was reduced in PLA1A knockdown cells. Mechanistically, PLA1A was required in TBK1-mitochondrial antiviral signaling protein (MAVS) interactions but not the interactions of TBK1 with other adaptor proteins. Furthermore, PLA1A knockdown reduced the recruitment of TBK1 and IRF3 to mitochondria, concomitant with altered mitochondria morphology.
journal_name
J Innate Immunjournal_title
Journal of innate immunityauthors
Gao X,Chen D,Hu X,Zhou Y,Wang Y,Wu C,Chen J,Wang Y,Pei R,Chen Xdoi
10.1159/000489832subject
Has Abstractpub_date
2018-01-01 00:00:00pages
315-327issue
4eissn
1662-811Xissn
1662-8128pii
000489832journal_volume
10pub_type
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
pub_type: 杂志文章
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
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doi:10.1159/000371423
更新日期:2015-01-01 00:00:00
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doi:10.1159/000228159
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
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journal_title:Journal of innate immunity
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