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10.1016/j.devcel.2015.03.007 http://scihub22266oqcxt.onion/10.1016/j.devcel.2015.03.007 C4421094!4421094!25942624     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       Dev+Cell 2015 ; 33 (3): 328-42 Nephropedia Template TP {{tp|p=25942624|t=2015. A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies |pdf=|usr=}}{{25942624}} gab.com Text A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies JO: Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=25942624 #FOAvip The abundance of cell surface membrane proteins is regulated by internalization and delivery into intralumenal vesicles (ILVs) of multivesicular bodies (MVB). Many cargoes are ubiquitinated, allowing access to an ESCRT-dependent pathway into MVBs. Yet, how non-ubiquitinated proteins, such as Glycosylphosphatidylinisotol-anchored proteins, enter MVBs is unclear, supporting the possibility of mechanistically distinct ILV biogenesis pathways. Here we show a family of highly ubiquitinated tetraspan Cos proteins provide a Ub-signal in trans, allowing sorting of non-ubiquitinated MVB cargo into the canonical ESCRT- and Ub-dependent pathway. Cos proteins create discrete endosomal subdomains that concentrate Ub-cargo prior to their envelopment into ILVs and the activity of Cos proteins is required not only for efficient sorting of canonical Ub-cargo but is also essential for sorting non-ubiquitinated cargo into MVBs. Expression of these proteins increases during nutrient stress though a NAD+/Sir2-dpendent mechanism that in turn accelerates the down-regulation of a broad range of cell surface proteins. Twit Text FOAVip A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies ????Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=25942624 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25942624 #FOAvip English Wikipedia <ref>{{Cite pmid|25942624}}</ref> A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies #MMPMID25942624 MacDonald C; Payne JA; Aboian M; Smith W; Katzmann DJ; Piper RC Dev Cell 2015[May]; 33 (3): 328-42 PMID25942624show ga The abundance of cell surface membrane proteins is regulated by internalization and delivery into intralumenal vesicles (ILVs) of multivesicular bodies (MVB). Many cargoes are ubiquitinated, allowing access to an ESCRT-dependent pathway into MVBs. Yet, how non-ubiquitinated proteins, such as Glycosylphosphatidylinisotol-anchored proteins, enter MVBs is unclear, supporting the possibility of mechanistically distinct ILV biogenesis pathways. Here we show a family of highly ubiquitinated tetraspan Cos proteins provide a Ub-signal in trans, allowing sorting of non-ubiquitinated MVB cargo into the canonical ESCRT- and Ub-dependent pathway. Cos proteins create discrete endosomal subdomains that concentrate Ub-cargo prior to their envelopment into ILVs and the activity of Cos proteins is required not only for efficient sorting of canonical Ub-cargo but is also essential for sorting non-ubiquitinated cargo into MVBs. Expression of these proteins increases during nutrient stress though a NAD+/Sir2-dpendent mechanism that in turn accelerates the down-regulation of a broad range of cell surface proteins. äA Family of Tetraspans Organizes Cargo for Sorting into Multivesicular(epmc).pdf DeepDyve Pubget Overpricing