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dc.contributor.author배옥남-
dc.date.accessioned2019-03-08T02:22:10Z-
dc.date.available2019-03-08T02:22:10Z-
dc.date.issued2015-03-
dc.identifier.citationCYTOKINE, v. 72, No. 1, Page. 63-70en_US
dc.identifier.issn1043-4666-
dc.identifier.urihttp://www.sciencedirect.com/science/article/pii/S104346661400622X-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/100620-
dc.description.abstractRetinoic acid-inducible gene I (RIG-I) plays an important role in antiviral immunity as a cytosolic receptor recognizing invading viruses. The activation of downstream signaling pathways led by IFN-beta promoter stimulator-1 (IPS-1), an adaptor, is known to culminate in the activation of IRFs and the expression of type I interferons. However, the role of Src-family-tyrosine kinases (STKs) in the RIG-I signaling pathway has not been fully evaluated. Through a combined approach of immunoprecipitation and micro reversed phase liquid chromatography-tandem mass spectrometry (RPLC-MS/MS) analysis, we established that Lyn, one of the STKs, is associated with RIG-I in macrophages. The association of Lyn and RIG-I was confirmed by co-immunoprecipitation study with 293T cells overexpressing Lyn and RIG-I. Suppression of Lyn by siRNA knockdown or a pharmacological inhibitor (PP2) resulted in the attenuation of IRF3 activation and IFN-beta expression induced by short poly I:C, a RIG-I agonist, in macrophages. Lyn activation, as determined by phosphorylation of Tyr396 residue, was observed upon short poly I:C stimulation in the mitochondria of macrophages. Short poly I:C induced the formation of speckle-like aggregates of Lyn, which are prominent in mitochondria. Lyn associated with IPS-1, an adaptor protein of RIG-I, which resides on mitochondria membrane. Helicase domain of RIG-I and CARD of IPS-1 are responsible for the interaction with Lyn while SH3 and SH2 domains in Lyn are required for the association with RIG-I and IPS-1. Collectively, our results indicate that Lyn plays a positive regulatory role in RIG-I-mediated interferon expression as a downstream component of IPS-1. They provide further information as to how tyrosine kinases such as STKs play a role in the regulation of antiviral immunity. (C) 2014 Elsevier Ltd. All rights reserved.en_US
dc.description.sponsorshipWe thank Sun Myung Joung, Min Jin Kim, and Sang Hyeon Yeon for their technical assistance. This study was supported by a grant from the National R&D Program for Cancer Control, Ministry of Health & Welfare, Republic of Korea (No. 1120120), a grant from the National Research Foundation of Korea (NRF) funded by the Korean government (No. 2012R1A1A3004541), and the Research Fund, 2012 of the Catholic University of Korea.en_US
dc.language.isoen_USen_US
dc.publisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTDen_US
dc.subjectInnate immunityen_US
dc.subjectAnti-viral signalingen_US
dc.subjectSrc-family-tyrosine kinasesen_US
dc.subjectIRF3en_US
dc.subjectType I interferonen_US
dc.titleA Src-family-tyrosine kinase, Lyn, is required for efficient IFN-beta, expression in pattern recognition receptor, RIG-I, signal pathway by interacting with IPS-1en_US
dc.typeArticleen_US
dc.relation.no1-
dc.relation.volume72-
dc.identifier.doi10.1016/j.cyto.2014.12.008.-
dc.relation.page63-70-
dc.relation.journalCYTOKINE-
dc.contributor.googleauthorKim, YJ-
dc.contributor.googleauthorKoo, JE-
dc.contributor.googleauthorHong, EH-
dc.contributor.googleauthorPark, ZY-
dc.contributor.googleauthorLim, KM-
dc.contributor.googleauthorBae, ON-
dc.contributor.googleauthorLee, JY-
dc.relation.code2015000829-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF PHARMACY[E]-
dc.sector.departmentDEPARTMENT OF PHARMACY-
dc.identifier.pidonbae-
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COLLEGE OF PHARMACY[E](약학대학) > PHARMACY(약학과) > Articles
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