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10.1074/jbc.M113.464776 http://scihub22266oqcxt.onion/10.1074/jbc.M113.464776 23965991!3789979!23965991     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2013 ; 288 (40): 28831-44 Nephropedia Template TP {{tp|p=23965991|t=2013. Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor |pdf=|usr=}}{{23965991}} gab.com Text Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23965991 #FOAvip The adenosine A2A receptor is a prototypical rhodopsin-like G protein-coupled receptor but has several unique structural features, in particular a long C terminus (of >120 residues) devoid of a palmitoylation site. It is known to interact with several accessory proteins other than those canonically involved in signaling. However, it is evident that many more proteins must interact with the A2A receptor, if the trafficking trajectory of the receptor is taken into account from its site of synthesis in the endoplasmic reticulum (ER) to its disposal by the lysosome. Affinity-tagged versions of the A2A receptor were expressed in HEK293 cells to identify interacting partners residing in the ER by a proteomics approach based on tandem affinity purification. The receptor-protein complexes were purified in quantities sufficient for analysis by mass spectrometry. We identified molecular chaperones (heat-shock proteins HSP90alpha and HSP70-1A) that interact with and retain partially folded A2A receptor prior to ER exit. Complex formation between the A2A receptor and HSP90alpha (but not HSP90beta) and HSP70-1A was confirmed by co-affinity precipitation. HSP90 inhibitors also enhanced surface expression of the receptor in PC12 cells, which endogenously express the A2A receptor. Finally, proteins of the HSP relay machinery (e.g. HOP/HSC70-HSP90 organizing protein and P23/HSP90 co-chaperone) were recovered in complexes with the A2A receptor. These observations are consistent with the proposed chaperone/coat protein complex II exchange model. This posits that cytosolic HSP proteins are sequentially recruited to folding intermediates of the A2A receptor. Release of HSP90 is required prior to recruitment of coat protein complex II components. This prevents premature ER export of partially folded receptors. Twit Text FOAVip Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23965991 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23965991 #FOAvip English Wikipedia <ref>{{Cite pmid|23965991}}</ref> Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor #MMPMID23965991 Bergmayr C; Thurner P; Keuerleber S; Kudlacek O; Nanoff C; Freissmuth M; Gruber CW J Biol Chem 2013[Oct]; 288 (40): 28831-44 PMID23965991show ga The adenosine A2A receptor is a prototypical rhodopsin-like G protein-coupled receptor but has several unique structural features, in particular a long C terminus (of >120 residues) devoid of a palmitoylation site. It is known to interact with several accessory proteins other than those canonically involved in signaling. However, it is evident that many more proteins must interact with the A2A receptor, if the trafficking trajectory of the receptor is taken into account from its site of synthesis in the endoplasmic reticulum (ER) to its disposal by the lysosome. Affinity-tagged versions of the A2A receptor were expressed in HEK293 cells to identify interacting partners residing in the ER by a proteomics approach based on tandem affinity purification. The receptor-protein complexes were purified in quantities sufficient for analysis by mass spectrometry. We identified molecular chaperones (heat-shock proteins HSP90alpha and HSP70-1A) that interact with and retain partially folded A2A receptor prior to ER exit. Complex formation between the A2A receptor and HSP90alpha (but not HSP90beta) and HSP70-1A was confirmed by co-affinity precipitation. HSP90 inhibitors also enhanced surface expression of the receptor in PC12 cells, which endogenously express the A2A receptor. Finally, proteins of the HSP relay machinery (e.g. HOP/HSC70-HSP90 organizing protein and P23/HSP90 co-chaperone) were recovered in complexes with the A2A receptor. These observations are consistent with the proposed chaperone/coat protein complex II exchange model. This posits that cytosolic HSP proteins are sequentially recruited to folding intermediates of the A2A receptor. Release of HSP90 is required prior to recruitment of coat protein complex II components. This prevents premature ER export of partially folded receptors. |*Signal Transduction/drug effects[MESH] |Animals[MESH] |Cytoplasm/drug effects/*metabolism[MESH] |HEK293 Cells[MESH] |HSP70 Heat-Shock Proteins/*metabolism[MESH] |HSP90 Heat-Shock Proteins/antagonists & inhibitors/*metabolism[MESH] |Humans[MESH] |Immunoprecipitation[MESH] |Intramolecular Oxidoreductases/metabolism[MESH] |Mass Spectrometry[MESH] |PC12 Cells[MESH] |Prostaglandin-E Synthases[MESH] |Proteasome Endopeptidase Complex/metabolism[MESH] |Proteasome Inhibitors/pharmacology[MESH] |Protein Binding/drug effects[MESH] |Protein Folding/drug effects[MESH] |RNA, Small Interfering/metabolism[MESH] |Rats[MESH] |Receptor, Adenosine A2A/*metabolism[MESH] |Recombinant Fusion Proteins/isolation & purification/metabolism[MESH] |Solubility[MESH]Recruitment of a cytoplasmic chaperone relay by the A2A adenosine rece(epmc).pdf DeepDyve Pubget Overpricing