Innate immunity at mucosal surfaces: the IRE1-RIDD-RIG-I pathway
作者： Wayne I. Lencer , Heidi DeLuca , Michael J. Grey , Jin Ah Cho
关键词: Unfolded protein response 、 RIG-I 、 Inflammation 、 Biology 、 Endoplasmic reticulum 、 Receptor 、 DEAD Box Protein 58 、 Innate immune system 、 Pattern recognition receptor 、 Immunology
摘要: Recent studies have linked the ER stress sensor IRE1α with RIG-I pathway, which triggers an inflammatory response upon detection of viral RNAs. In to dysfunction, cleaves mRNA into single-strand fragments that lack markers self, activate RIG-I. Certain microbial products from mucosal pathogens this pathway by binding directly, and discovery IRE1 is amplified at surfaces gene duplication suggests important role for in immunity. Here, we review evidence support hypothesis, propose a model wherein surveys integrity ER, acting as guard receptor pattern recognition receptor, capable both sensing cellular caused infection responding directly.
unirioja.es
elsevier.com
sci-hub.se 参考文章(107)
A.-H. Lee, E. F. Scapa, D. E. Cohen, L. H. Glimcher, Regulation of hepatic lipogenesis by the transcription factor XBP1 Science. ,vol. 320, pp. 1492- 1496 ,(2008) , 10.1126/SCIENCE.1158042
Tetsushi Kawahara, Hideki Yanagi, Takashi Yura, Kazutoshi Mori, Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response Molecular Biology of the Cell. ,vol. 8, pp. 1845- 1862 ,(1997) , 10.1091/MBC.8.10.1845
Chao Zheng, Hao Wu, RIG-I “Sees” the 5′-Triphosphate Structure. ,vol. 18, pp. 894- 896 ,(2010) , 10.1016/J.STR.2010.07.002
K. Kohno, Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals. Journal of Biochemistry. ,vol. 147, pp. 27- 33 ,(2010) , 10.1093/JB/MVP196
J.-P. Upton, L. Wang, D. Han, E. S. Wang, N. E. Huskey, L. Lim, M. Truitt, M. T. McManus, D. Ruggero, A. Goga, F. R. Papa, S. A. Oakes, IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2 Science. ,vol. 338, pp. 818- 822 ,(2012) , 10.1126/SCIENCE.1226191
Kezhong Zhang, Randal J. Kaufman, From endoplasmic-reticulum stress to the inflammatory response Nature. ,vol. 454, pp. 455- 462 ,(2008) , 10.1038/NATURE07203
J. J. Credle, J. S. Finer-Moore, F. R. Papa, R. M. Stroud, P. Walter, On the mechanism of sensing unfolded protein in the endoplasmic reticulum Proceedings of the National Academy of Sciences of the United States of America. ,vol. 102, pp. 18773- 18784 ,(2005) , 10.1073/PNAS.0509487102
Davide Eletto, Daniela Eletto, Devin Dersh, Tali Gidalevitz, Yair Argon, Protein Disulfide Isomerase A6 Controls the Decay of IRE1α Signaling via Disulfide-Dependent Association Molecular Cell. ,vol. 53, pp. 562- 576 ,(2014) , 10.1016/J.MOLCEL.2014.01.004
Richard Jäger, Mathieu J.M. Bertrand, Adrienne M. Gorman, Peter Vandenabeele, Afshin Samali, The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress Biology of the Cell. ,vol. 104, pp. 259- 270 ,(2012) , 10.1111/BOC.201100055
Yusuke Imagawa, Akira Hosoda, Shin-ichi Sasaka, Akio Tsuru, Kenji Kohno, RNase domains determine the functional difference between IRE1α and IRE1β FEBS Letters. ,vol. 582, pp. 656- 660 ,(2008) , 10.1016/J.FEBSLET.2008.01.038