Analysis of the uptake mechanism for double stranded RNA

我们发现胞质脂筏蛋白Raftlin对于人髓样DC和上皮细胞中的poly（I：C）细胞摄取是必需的。当Raftlin被沉默时，poly（I：C）不能进入细胞并且IFN-β产生的诱导被抑制。此外，细胞摄取的B型寡脱氧核苷酸，共享其摄取受体与聚（I：C）抑制Raftlin敲除细胞。在poly（I：C）刺激后，Raftlin从细胞质易位到质膜，在那里它与poly（I：C）共定位，然后移动到TLR 3阳性内体。因此，Raftlin与摄取受体合作介导poly（I：C）进入细胞，这对TLR 3的活化至关重要。

we show that the cytoplasmic lipid raft protein, Raftlin, is essential for poly(I:C) cellular uptake in human myeloid DCs and epithelial cells. When Raftlin was silenced, poly(I:C) failed to enter cells and induction of IFN-beta 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.