Abstract:
:The innate immune system senses cytosolic dsDNA and bacterial cyclic dinucleotides and initiates signaling via the adaptor STING to induce type 1 interferon (IFN) response. We demonstrate here that BTK-deficient cells have impaired IFN-β production and TBK1/IRF3 activation when stimulated with agonists or infected with pathogens that activate STING signaling. BTK interacts with STING and DDX41 helicase. The kinase and SH3/SH2 interaction domains of BTK bind, respectively, the DEAD-box domain of DDX41 and transmembrane region of STING. BTK phosphorylates DDX41, and its kinase activities are critical for STING-mediated IFN-β production. We show that Tyr364 and Tyr414 of DDX41 are critical for its recognition of AT-rich DNA and binding to STING, and tandem mass spectrometry identifies Tyr414 as the BTK phosphorylation site. Modeling studies further indicate that phospho-Tyr414 strengthens DDX41's interaction with STING. Hence, BTK plays a critical role in the activation of DDX41 helicase and STING signaling.
journal_name
Cell Repjournal_title
Cell reportsauthors
Lee KG,Kim SS,Kui L,Voon DC,Mauduit M,Bist P,Bi X,Pereira NA,Liu C,Sukumaran B,Rénia L,Ito Y,Lam KPdoi
10.1016/j.celrep.2015.01.039subject
Has Abstractpub_date
2015-02-24 00:00:00pages
1055-65issue
7issn
2211-1247pii
S2211-1247(15)00064-9journal_volume
10pub_type
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