Source:http://linkedlifedata.com/resource/pubmed/id/21266579
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2011-4-1
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pubmed:abstractText |
The double-stranded RNA analog, poly(I:C), extracellularly activates both the endosomal Toll-like receptor (TLR) 3 and the cytoplasmic RNA helicase, melanoma differentiation-associated gene 5, leading to the production of type I interferons (IFNs) and inflammatory cytokines. The mechanism by which extracellular poly(I:C) is delivered to TLR3-positive organelles and the cytoplasm remains to be elucidated. Here, we show that the cytoplasmic lipid raft protein, Raftlin, is essential for poly(I:C) cellular uptake in human myeloid dendritic cells and epithelial cells. When Raftlin was silenced, poly(I:C) failed to enter cells and induction of IFN-? production was inhibited. In addition, cellular uptake of B-type oligodeoxynucleotide that shares its uptake receptor with poly(I:C) was suppressed in Raftlin knockdown cells. Upon poly(I:C) stimulation, Raftlin was translocated from the cytoplasm to the plasma membrane where it colocalized with poly(I:C), and thereafter moved to TLR3-positive endosomes. Thus, Raftlin cooperates with the uptake receptor to mediate cell entry of poly(I:C), which is critical for activation of TLR3.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Inducers,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Poly I-C,
http://linkedlifedata.com/resource/pubmed/chemical/RAFTLIN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TLR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TLR3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 3
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10702-11
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pubmed:meshHeading |
pubmed-meshheading:21266579-Animals,
pubmed-meshheading:21266579-Cell Line, Tumor,
pubmed-meshheading:21266579-Cell Membrane,
pubmed-meshheading:21266579-Dendritic Cells,
pubmed-meshheading:21266579-Endosomes,
pubmed-meshheading:21266579-Gene Silencing,
pubmed-meshheading:21266579-HEK293 Cells,
pubmed-meshheading:21266579-Humans,
pubmed-meshheading:21266579-Interferon Inducers,
pubmed-meshheading:21266579-Interferon-beta,
pubmed-meshheading:21266579-Membrane Proteins,
pubmed-meshheading:21266579-Mice,
pubmed-meshheading:21266579-Mice, Knockout,
pubmed-meshheading:21266579-Myeloid Cells,
pubmed-meshheading:21266579-Poly I-C,
pubmed-meshheading:21266579-Toll-Like Receptor 3
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pubmed:year |
2011
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pubmed:articleTitle |
Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation.
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pubmed:affiliation |
Department of Microbiology and Immunology, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo 060-8638, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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