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10.1074/jbc.M113.469882 http://scihub22266oqcxt.onion/10.1074/jbc.M113.469882 C3689978!3689978 !23645669     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23645669 &cmd=llinks): Failed to open stream: HTTP request failed! 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The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel |pdf=|usr=}}{{23645669 }} gab.com Text The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23645669 #FOAvip The epithelial sodium channel, ENaC, plays a critical role in maintaining salt and water homeostasis, and not surprisingly defects in ENaC function are associated with disease. Like many other membrane-spanning proteins, this trimeric protein complex folds and assembles inefficiently in the endoplasmic reticulum (ER), which results in a substantial percentage of the channel being targeted for ER-associated degradation (ERAD). Because the spectrum of factors that facilitates the degradation of ENaC is incomplete, we developed yeast expression systems for each ENaC subunit. We discovered that a conserved Hsp70-like chaperone, Lhs1, is required for maximal turnover of the ENaC ? subunit. By expressing Lhs1 ATP binding mutants, we also found that the nucleotide exchange properties of this chaperone are dispensable for ENaC degradation. Consistent with the precipitation of an Lhs1-?ENaC complex, Lhs1 holdase activity was instead most likely required to support the ERAD of ?ENaC. Moreover, a complex containing the mammalian Lhs1 homolog GRP170 and ?ENaC co-precipitated, and GRP170 also facilitated ENaC degradation in human, HEK293 cells, and in a Xenopus oocyte expression system. In both yeast and higher cell types, the effect of Lhs1 on the ERAD of ?ENaC was selective for the unglycosylated form of the protein. These data establish the first evidence that Lhs1/Grp170 chaperones can act as mediators of ERAD substrate selection. Twit Text FOAVip The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23645669 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23645669 #FOAvip English Wikipedia <ref>{{Cite pmid|23645669 }}</ref> The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel #MMPMID23645669 Buck TM ; Plavchak L ; Roy A ; Donnelly BF ; Kashlan OB ; Kleyman TR ; Subramanya AR ; Brodsky JL J Biol Chem 2013[Jun]; 288 (25 ): 18366-80 PMID23645669 show ga The epithelial sodium channel, ENaC, plays a critical role in maintaining salt and water homeostasis, and not surprisingly defects in ENaC function are associated with disease. Like many other membrane-spanning proteins, this trimeric protein complex folds and assembles inefficiently in the endoplasmic reticulum (ER), which results in a substantial percentage of the channel being targeted for ER-associated degradation (ERAD). Because the spectrum of factors that facilitates the degradation of ENaC is incomplete, we developed yeast expression systems for each ENaC subunit. We discovered that a conserved Hsp70-like chaperone, Lhs1, is required for maximal turnover of the ENaC ? subunit. By expressing Lhs1 ATP binding mutants, we also found that the nucleotide exchange properties of this chaperone are dispensable for ENaC degradation. Consistent with the precipitation of an Lhs1-?ENaC complex, Lhs1 holdase activity was instead most likely required to support the ERAD of ?ENaC. Moreover, a complex containing the mammalian Lhs1 homolog GRP170 and ?ENaC co-precipitated, and GRP170 also facilitated ENaC degradation in human, HEK293 cells, and in a Xenopus oocyte expression system. In both yeast and higher cell types, the effect of Lhs1 on the ERAD of ?ENaC was selective for the unglycosylated form of the protein. These data establish the first evidence that Lhs1/Grp170 chaperones can act as mediators of ERAD substrate selection. |*Endoplasmic Reticulum-Associated Degradation [MESH] |Adenosine Triphosphate/metabolism [MESH] |Amiloride/pharmacology [MESH] |Animals [MESH] |Endoplasmic Reticulum/metabolism [MESH] |Epithelial Sodium Channels/genetics/*metabolism [MESH] |Female [MESH] |Glycoproteins/genetics/*metabolism [MESH] |HEK293 Cells [MESH] |HSP70 Heat-Shock Proteins/genetics/*metabolism [MESH] |Humans [MESH] |Immunoblotting [MESH] |Ion Transport/drug effects [MESH] |Membrane Potentials/drug effects [MESH] |Mutation [MESH] |Oocytes/metabolism/physiology [MESH] |Protein Binding [MESH] |Saccharomyces cerevisiae Proteins/genetics/*metabolism [MESH] |Saccharomyces cerevisiae/genetics/metabolism [MESH] |Sodium/metabolism [MESH]The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associ(epmc).pdf DeepDyve Pubget Overpricing