Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1210/me.2010-0072 http://scihub22266oqcxt.onion/10.1210/me.2010-0072 C5417385!5417385 !20843941     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=20843941 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\20843941 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Endocrinol 2010 ; 24 (11 ): 2179-92 Nephropedia Template TP {{tp|p=20843941 |t=2010. A novel domain mediates insulin-induced proteasomal degradation of insulin receptor substrate 1 (IRS-1) |pdf=|usr=}}{{20843941 }} gab.com Text A novel domain mediates insulin-induced proteasomal degradation of insulin receptor substrate 1 (IRS-1) JO: Mol Endocrinol http://www.kidney.de/pget.php?&tw=1&pmid=20843941 #FOAvip Insulin receptor substrate-1 (IRS-1) plays a pivotal role in insulin signaling, therefore its degradation is exquisitely regulated. Here, we show that insulin-stimulated degradation of IRS-1 requires the presence of a highly conserved Ser/Thr-rich domain that we named domain involved in degradation of IRS-1 (DIDI). DIDI (amino acids 386-430 of IRS-1) was identified by comparing the intracellular degradation rate of several truncated forms of IRS-1 transfected into CHO cells. The isolated DIDI domain underwent insulin-stimulated Ser/Thr phosphorylation, suggesting that it serves as a target for IRS-1 kinases. The effects of deletion of DIDI were studied in Fao rat hepatoma and in CHO cells expressing Myc-IRS-1(WT) or Myc-IRS-1(?386-430). Deletion of DIDI maintained the ability of IRS-1(?386-434) to undergo ubiquitination while rendering it insensitive to insulin-induced proteasomal degradation, which affected IRS-1(WT) (80% at 8 h). Consequently, IRS-1(?386-434) mediated insulin signaling (activation of Akt and glycogen synthesis) better than IRS-1(WT). IRS-1(?386-434) exhibited a significant greater preference for nuclear localization, compared with IRS-1(WT). Higher nuclear localization was also observed when cells expressing IRS-1(WT) were incubated with the proteasome inhibitor MG-132. The sequence of DIDI is conserved more than 93% across species, from fish to mammals, as opposed to approximately 40% homology of the entire IRS-1. These findings implicate DIDI as a novel, highly conserved domain of IRS-1, which mediates its cellular localization, rate of degradation, and biological activity, with a direct impact on insulin signal transduction. Twit Text FOAVip A novel domain mediates insulin-induced proteasomal degradation of insulin receptor substrate 1 (IRS-1) ????Mol Endocrinol http://www.kidney.de/pget.php?&tw=1&pmid=20843941 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=20843941 #FOAvip English Wikipedia <ref>{{Cite pmid|20843941 }}</ref> A novel domain mediates insulin-induced proteasomal degradation of insulin receptor substrate 1 (IRS-1) #MMPMID20843941 Boura-Halfon S ; Shuster-Meiseles T ; Beck A ; Petrovich K ; Gurevitch D ; Ronen D ; Zick Y Mol Endocrinol 2010[Nov]; 24 (11 ): 2179-92 PMID20843941 show ga Insulin receptor substrate-1 (IRS-1) plays a pivotal role in insulin signaling, therefore its degradation is exquisitely regulated. Here, we show that insulin-stimulated degradation of IRS-1 requires the presence of a highly conserved Ser/Thr-rich domain that we named domain involved in degradation of IRS-1 (DIDI). DIDI (amino acids 386-430 of IRS-1) was identified by comparing the intracellular degradation rate of several truncated forms of IRS-1 transfected into CHO cells. The isolated DIDI domain underwent insulin-stimulated Ser/Thr phosphorylation, suggesting that it serves as a target for IRS-1 kinases. The effects of deletion of DIDI were studied in Fao rat hepatoma and in CHO cells expressing Myc-IRS-1(WT) or Myc-IRS-1(?386-430). Deletion of DIDI maintained the ability of IRS-1(?386-434) to undergo ubiquitination while rendering it insensitive to insulin-induced proteasomal degradation, which affected IRS-1(WT) (80% at 8 h). Consequently, IRS-1(?386-434) mediated insulin signaling (activation of Akt and glycogen synthesis) better than IRS-1(WT). IRS-1(?386-434) exhibited a significant greater preference for nuclear localization, compared with IRS-1(WT). Higher nuclear localization was also observed when cells expressing IRS-1(WT) were incubated with the proteasome inhibitor MG-132. The sequence of DIDI is conserved more than 93% across species, from fish to mammals, as opposed to approximately 40% homology of the entire IRS-1. These findings implicate DIDI as a novel, highly conserved domain of IRS-1, which mediates its cellular localization, rate of degradation, and biological activity, with a direct impact on insulin signal transduction. |Animals [MESH] |Apoptosis/drug effects [MESH] |CHO Cells [MESH] |Cricetinae [MESH] |Cricetulus [MESH] |Cytoprotection/drug effects [MESH] |Insulin Receptor Substrate Proteins/*chemistry/*metabolism [MESH] |Insulin/*pharmacology [MESH] |Mice [MESH] |Mutant Proteins/chemistry/metabolism [MESH] |Phosphorylation/drug effects [MESH] |Phosphoserine/metabolism [MESH] |Proteasome Endopeptidase Complex/*metabolism [MESH] |Protein Processing, Post-Translational/*drug effects [MESH] |Protein Structure, Tertiary [MESH] |Protein Transport/drug effects [MESH] |Proto-Oncogene Proteins c-mdm2/metabolism [MESH] |Rats [MESH] |Sequence Deletion [MESH] |Signal Transduction/drug effects [MESH] |Structure-Activity Relationship [MESH]A novel domain mediates insulin-induced proteasomal degradation of ins(epmc).pdf DeepDyve Pubget Overpricing