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10.1073/pnas.1615163114 http://scihub22266oqcxt.onion/10.1073/pnas.1615163114 C5380026!5380026!28289207     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       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (13): 3433-8 Nephropedia Template TP {{tp|p=28289207|t=2017. Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans-Golgi network |pdf=|usr=}}{{28289207}} gab.com Text Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans-Golgi network JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28289207 #FOAvip Clathrin-coated vesicles (ccv) are fundamental intracellular transport carriers in eukaryotic cells. Assembly of ccv at appropriate intracellular membrane sites requires membrane-associated factors, including phosphoinositide lipids that recruit clathrin adaptors to the membrane to initiate ccv formation. How levels of specific phosphoinositides are controlled at particular membranes is not well understood. At the trans-Golgi network (TGN), the key phosphoinositide is phosphatidylinositol 4-phosphate (PtdIns4P). Here we characterize molecular interactions between Gga (Golgi-localized, gamma-adaptin ear homology, Arf-binding) clathrin adaptors and a kinase responsible for PtdIns4P synthesis at the TGN in yeast and mammalian cells. Defects that reduce kinase binding to Gga proteins inhibit kinase recruitment to the TGN. These results identify an evolutionarily conserved role for Gga clathrin adaptors in controlling PtdIns4P synthesis at the TGN. Twit Text FOAVip Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans-Golgi network ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28289207 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28289207 #FOAvip English Wikipedia <ref>{{Cite pmid|28289207}}</ref> Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans-Golgi network #MMPMID28289207 Daboussi L; Costaguta G; Ghukasyan R; Payne GS Proc Natl Acad Sci U S A 2017[Mar]; 114 (13): 3433-8 PMID28289207show ga Clathrin-coated vesicles (ccv) are fundamental intracellular transport carriers in eukaryotic cells. Assembly of ccv at appropriate intracellular membrane sites requires membrane-associated factors, including phosphoinositide lipids that recruit clathrin adaptors to the membrane to initiate ccv formation. How levels of specific phosphoinositides are controlled at particular membranes is not well understood. At the trans-Golgi network (TGN), the key phosphoinositide is phosphatidylinositol 4-phosphate (PtdIns4P). Here we characterize molecular interactions between Gga (Golgi-localized, gamma-adaptin ear homology, Arf-binding) clathrin adaptors and a kinase responsible for PtdIns4P synthesis at the TGN in yeast and mammalian cells. Defects that reduce kinase binding to Gga proteins inhibit kinase recruitment to the TGN. These results identify an evolutionarily conserved role for Gga clathrin adaptors in controlling PtdIns4P synthesis at the TGN. äConserved role for Gga proteins in phosphatidylinositol 4-kinase local(epmc).pdf DeepDyve Pubget Overpricing