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10.1016/j.molcel.2014.04.030 http://scihub22266oqcxt.onion/10.1016/j.molcel.2014.04.030 C4445634!4445634!24882209     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24882209&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 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell 2014 ; 55 (1): 15-30 Nephropedia Template TP {{tp|p=24882209|t=2014. A cellular system that degrades misfolded proteins and protects against neurodegeneration |pdf=|usr=}}{{24882209}} gab.com Text A cellular system that degrades misfolded proteins and protects against neurodegeneration JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=24882209 #FOAvip The accumulation of misfolded proteins compromises cellular function and causes debilitating diseases. However, the cellular systems that detect and degrade these proteins remain poorly understood. Here we show that the tripartite motif protein PML/TRIM19 and the SUMO-dependent ubiquitin ligase RNF4 act together to promote the degradation of various misfolded proteins in mammalian cell nuclei. Mechanistically, PML selectively interacts with misfolded proteins through distinct substrate recognition sites, and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. SUMOylated misfolded proteins are subsequently recognized and ubiquitinated by RNF4 and targeted for proteasomal degradation. We further show that PML deficiency exacerbates polyglutamine (polyQ) disease in a mouse model of spinocerebellar ataxia 1 (SCA1). These findings reveal a system in mammalian cells that remove misfolded proteins through sequential PML-mediated SUMOylation and RNF4-mediated ubiquitination. They also suggest that the PML-RNF4 system may be a potential target for treating protein-misfolding diseases. Twit Text FOAVip A cellular system that degrades misfolded proteins and protects against neurodegeneration ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=24882209 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24882209 #FOAvip English Wikipedia <ref>{{Cite pmid|24882209}}</ref> A cellular system that degrades misfolded proteins and protects against neurodegeneration #MMPMID24882209 Guo L; Giasson BI; Glavis-Bloom A; Brewer MD; Shorter J; Gitler AD; Yang X Mol Cell 2014[Jul]; 55 (1): 15-30 PMID24882209show ga The accumulation of misfolded proteins compromises cellular function and causes debilitating diseases. However, the cellular systems that detect and degrade these proteins remain poorly understood. Here we show that the tripartite motif protein PML/TRIM19 and the SUMO-dependent ubiquitin ligase RNF4 act together to promote the degradation of various misfolded proteins in mammalian cell nuclei. Mechanistically, PML selectively interacts with misfolded proteins through distinct substrate recognition sites, and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. SUMOylated misfolded proteins are subsequently recognized and ubiquitinated by RNF4 and targeted for proteasomal degradation. We further show that PML deficiency exacerbates polyglutamine (polyQ) disease in a mouse model of spinocerebellar ataxia 1 (SCA1). These findings reveal a system in mammalian cells that remove misfolded proteins through sequential PML-mediated SUMOylation and RNF4-mediated ubiquitination. They also suggest that the PML-RNF4 system may be a potential target for treating protein-misfolding diseases. äA cellular system that degrades misfolded proteins and protects agains(epmc).pdf DeepDyve Pubget Overpricing