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10.1016/j.isci.2021.102770 http://scihub22266oqcxt.onion/10.1016/j.isci.2021.102770 34189428!8223119!34189428     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       iScience 2021 ; 24 (7): 102770 Nephropedia Template TP {{tp|p=34189428|t=2021. ACE2 interaction with cytoplasmic PDZ protein enhances SARS-CoV-2 invasion |pdf=|usr=}}{{34189428}} gab.com Text ACE2 interaction with cytoplasmic PDZ protein enhances SARS-CoV-2 invasion JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=34189428 #FOAvip SARS-CoV-2 is responsible for the global COVID-19 pandemic. Angiotensin converting enzyme 2 (ACE2) is the membrane-delimited receptor for SARS-CoV-2. Lung, intestine, and kidney, major sites of viral infection, express ACE2 that harbors an intracellular, carboxy-terminal PDZ-recognition motif. These organs prominently express the PDZ protein Na(+)/H(+) exchanger regulatory factor-1 (NHERF1). Here, we report NHERF1 tethers ACE2 and augments SARS-CoV-2 cell entry. ACE2 directly binds both NHERF1 PDZ domains. Disruption of either NHERF1 PDZ core-binding motif or the ACE2 PDZ recognition sequence eliminates interaction. Proximity ligation assays establish that ACE2 and NHERF1 interact at constitutive expression levels in human lung and intestine cells. Ablating ACE2 interaction with NHERF1 accelerated SARS-CoV-2 cell entry. Conversely, elimination of the ACE2 C-terminal PDZ-binding motif decreased ACE2 membrane residence and reduced pseudotyped virus entry. We conclude that the PDZ interaction of ACE2 with NHERF1 facilitates SARS-CoV-2 internalization. beta-Arrestin is likely indispensable, as with G protein-coupled receptors. Twit Text FOAVip ACE2 interaction with cytoplasmic PDZ protein enhances SARS-CoV-2 invasion ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=34189428 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34189428 #FOAvip English Wikipedia <ref>{{Cite pmid|34189428}}</ref> ACE2 interaction with cytoplasmic PDZ protein enhances SARS-CoV-2 invasion #MMPMID34189428 Zhang Q; Gefter J; Sneddon WB; Mamonova T; Friedman PA iScience 2021[Jul]; 24 (7): 102770 PMID34189428show ga SARS-CoV-2 is responsible for the global COVID-19 pandemic. Angiotensin converting enzyme 2 (ACE2) is the membrane-delimited receptor for SARS-CoV-2. Lung, intestine, and kidney, major sites of viral infection, express ACE2 that harbors an intracellular, carboxy-terminal PDZ-recognition motif. These organs prominently express the PDZ protein Na(+)/H(+) exchanger regulatory factor-1 (NHERF1). Here, we report NHERF1 tethers ACE2 and augments SARS-CoV-2 cell entry. ACE2 directly binds both NHERF1 PDZ domains. Disruption of either NHERF1 PDZ core-binding motif or the ACE2 PDZ recognition sequence eliminates interaction. Proximity ligation assays establish that ACE2 and NHERF1 interact at constitutive expression levels in human lung and intestine cells. Ablating ACE2 interaction with NHERF1 accelerated SARS-CoV-2 cell entry. Conversely, elimination of the ACE2 C-terminal PDZ-binding motif decreased ACE2 membrane residence and reduced pseudotyped virus entry. We conclude that the PDZ interaction of ACE2 with NHERF1 facilitates SARS-CoV-2 internalization. beta-Arrestin is likely indispensable, as with G protein-coupled receptors. äACE2 interaction with cytoplasmic PDZ protein enhances SARS-CoV-2 inva(epmc).pdf DeepDyve Pubget Overpricing