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10.1111/cmi.12262 http://scihub22266oqcxt.onion/10.1111/cmi.12262 24521078!4065222!24521078     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Microbiol 2014 ; 16 (7): 1080-93 Nephropedia Template TP {{tp|p=24521078|t=2014. Identification of an endocytic signal essential for the antiviral action of IFITM3 |pdf=|usr=}}{{24521078}} gab.com Text Identification of an endocytic signal essential for the antiviral action of IFITM3 JO: Cell Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=24521078 #FOAvip Members of the interferon-induced transmembrane (IFITM) protein family inhibit the entry of a wide range of viruses. Viruses often exploit the endocytosis pathways to invade host cells and escape from the endocytic vesicles often in response to low pH. Localization to these endocytic vesicles is essential for IFITM3 to interfere with the cytosolic entry of pH-dependent viruses. However, the nature of the sorting signal that targets IFITM3 to these vesicles is poorly defined. In this study, we report that IFITM3 possesses a YxxPhi sorting motif, i.e. 20-YEML-23, that enables IFITM3 to undergo endocytosis through binding to the mu2 subunit of the AP-2 complex. IFITM3 accumulates at the plasma membrane as a result of either mutating 20-YEML-23, depleting the mu2 subunit or overexpressing mu2 mutants. Importantly, blocking endocytosis of IFITM3 abrogates its ability to inhibit pH-dependent viruses. We have therefore identified a critical sorting signal, namely 20-YEML-23, that controls both the endocytic trafficking and the antiviral action of IFITM3. This finding also reveals that as an endocytic protein, IFITM3 first arrives at the plasma membrane before it is endocytosed and further traffics to the late endosomes where it acts to impede virus entry. Twit Text FOAVip Identification of an endocytic signal essential for the antiviral action of IFITM3 ????Cell Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=24521078 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24521078 #FOAvip English Wikipedia <ref>{{Cite pmid|24521078}}</ref> Identification of an endocytic signal essential for the antiviral action of IFITM3 #MMPMID24521078 Jia R; Xu F; Qian J; Yao Y; Miao C; Zheng YM; Liu SL; Guo F; Geng Y; Qiao W; Liang C Cell Microbiol 2014[Jul]; 16 (7): 1080-93 PMID24521078show ga Members of the interferon-induced transmembrane (IFITM) protein family inhibit the entry of a wide range of viruses. Viruses often exploit the endocytosis pathways to invade host cells and escape from the endocytic vesicles often in response to low pH. Localization to these endocytic vesicles is essential for IFITM3 to interfere with the cytosolic entry of pH-dependent viruses. However, the nature of the sorting signal that targets IFITM3 to these vesicles is poorly defined. In this study, we report that IFITM3 possesses a YxxPhi sorting motif, i.e. 20-YEML-23, that enables IFITM3 to undergo endocytosis through binding to the mu2 subunit of the AP-2 complex. IFITM3 accumulates at the plasma membrane as a result of either mutating 20-YEML-23, depleting the mu2 subunit or overexpressing mu2 mutants. Importantly, blocking endocytosis of IFITM3 abrogates its ability to inhibit pH-dependent viruses. We have therefore identified a critical sorting signal, namely 20-YEML-23, that controls both the endocytic trafficking and the antiviral action of IFITM3. This finding also reveals that as an endocytic protein, IFITM3 first arrives at the plasma membrane before it is endocytosed and further traffics to the late endosomes where it acts to impede virus entry. |Adaptor Protein Complex 2/metabolism[MESH] |Adaptor Protein Complex mu Subunits/metabolism[MESH] |Amino Acid Motifs[MESH] |Cell Membrane/metabolism[MESH] |Conserved Sequence[MESH] |Endocytosis[MESH] |Endosomes/*metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Influenza A Virus, H1N1 Subtype/physiology[MESH] |Membrane Proteins/chemistry/*metabolism[MESH] |Molecular Sequence Data[MESH] |Protein Binding[MESH] |Protein Sorting Signals[MESH] |Protein Subunits[MESH] |Protein Transport[MESH] |RNA-Binding Proteins/chemistry/*metabolism[MESH]Identification of an endocytic signal essential for the antiviral acti(epmc).pdf DeepDyve Pubget Overpricing