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10.1038/s41467-021-25589-1 http://scihub22266oqcxt.onion/10.1038/s41467-021-25589-1 34504087!8429659!34504087     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2021 ; 12 (1): 5333 Nephropedia Template TP {{tp|p=34504087|t=2021. Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation |pdf=|usr=}}{{34504087}} gab.com Text Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34504087 #FOAvip The Spike (S) protein of SARS-CoV-2 binds ACE2 to direct fusion with host cells. S comprises a large external domain, a transmembrane domain, and a short cytoplasmic tail. Understanding the intracellular trafficking of S is relevant to SARS-CoV-2 infection, and to vaccines expressing full-length S from mRNA or adenovirus vectors. Here we report a proteomic screen for cellular factors that interact with the cytoplasmic tail of S. We confirm interactions with the COPI and COPII vesicle coats, ERM family actin regulators, and the WIPI3 autophagy component. The COPII binding site promotes exit from the endoplasmic reticulum, and although binding to COPI should retain S in the early Golgi where viral budding occurs, there is a suboptimal histidine residue in the recognition motif. As a result, S leaks to the surface where it accumulates and can direct the formation of multinucleate syncytia. Thus, the trafficking signals in the tail of S indicate that syncytia play a role in the SARS-CoV-2 lifecycle. Twit Text FOAVip Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34504087 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34504087 #FOAvip English Wikipedia <ref>{{Cite pmid|34504087}}</ref> Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation #MMPMID34504087 Cattin-Ortola J; Welch LG; Maslen SL; Papa G; James LC; Munro S Nat Commun 2021[Sep]; 12 (1): 5333 PMID34504087show ga The Spike (S) protein of SARS-CoV-2 binds ACE2 to direct fusion with host cells. S comprises a large external domain, a transmembrane domain, and a short cytoplasmic tail. Understanding the intracellular trafficking of S is relevant to SARS-CoV-2 infection, and to vaccines expressing full-length S from mRNA or adenovirus vectors. Here we report a proteomic screen for cellular factors that interact with the cytoplasmic tail of S. We confirm interactions with the COPI and COPII vesicle coats, ERM family actin regulators, and the WIPI3 autophagy component. The COPII binding site promotes exit from the endoplasmic reticulum, and although binding to COPI should retain S in the early Golgi where viral budding occurs, there is a suboptimal histidine residue in the recognition motif. As a result, S leaks to the surface where it accumulates and can direct the formation of multinucleate syncytia. Thus, the trafficking signals in the tail of S indicate that syncytia play a role in the SARS-CoV-2 lifecycle. |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Animals[MESH] |COP-Coated Vesicles/metabolism[MESH] |COVID-19/*metabolism[MESH] |Cell Membrane/*metabolism[MESH] |Chlorocebus aethiops[MESH] |Endoplasmic Reticulum/metabolism[MESH] |Giant Cells/*metabolism[MESH] |Golgi Apparatus/metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Proteomics[MESH] |SARS-CoV-2/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/*metabolism[MESH] |Vero Cells[MESH]Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expre(epmc).pdf DeepDyve Pubget Overpricing