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10.1038/s41467-018-03498-0 http://scihub22266oqcxt.onion/10.1038/s41467-018-03498-0 C5876331!5876331!29599493     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2018 ; 9 (ä): ä Nephropedia Template TP {{tp|p=29599493|t=2018. RING tetramerization is required for nuclear body biogenesis and PML sumoylation |pdf=|usr=}}{{29599493}} gab.com Text RING tetramerization is required for nuclear body biogenesis and PML sumoylation JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29599493 #FOAvip ProMyelocyticLeukemia nuclear bodies (PML NBs) are stress-regulated domains directly implicated in acute promyelocytic leukemia eradication. Most TRIM family members bind ubiquitin E2s and many acquire ligase activity upon RING dimerization. In contrast, PML binds UBC9, the SUMO E2 enzyme. Here, using X-ray crystallography and SAXS characterization, we demonstrate that PML RING tetramerizes through highly conserved PML-specific sequences, which are required for NB assembly and PML sumoylation. Conserved residues implicated in RING dimerization of other TRIMs also contribute to PML tetramer stability. Wild-type PML rescues the ability of some RING mutants to form NBs as well as their sumoylation. Impaired RING tetramerization abolishes PML/RARA-driven leukemogenesis in vivo and arsenic-induced differentiation ex vivo. Our studies thus identify RING tetramerization as a key step in the NB macro-molecular scaffolding. They suggest that higher order RING interactions allow efficient UBC9 recruitment and thus change the biochemical nature of TRIM-facilitated post-translational modifications. Twit Text FOAVip RING tetramerization is required for nuclear body biogenesis and PML sumoylation ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29599493 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29599493 #FOAvip English Wikipedia <ref>{{Cite pmid|29599493}}</ref> RING tetramerization is required for nuclear body biogenesis and PML sumoylation #MMPMID29599493 Wang P; Benhenda S; Wu H; Lallemand-Breitenbach V; Zhen T; Jollivet F; Peres L; Li Y; Chen SJ; Chen Z; de Thé H; Meng G Nat Commun 2018[]; 9 (ä): ä PMID29599493show ga ProMyelocyticLeukemia nuclear bodies (PML NBs) are stress-regulated domains directly implicated in acute promyelocytic leukemia eradication. Most TRIM family members bind ubiquitin E2s and many acquire ligase activity upon RING dimerization. In contrast, PML binds UBC9, the SUMO E2 enzyme. Here, using X-ray crystallography and SAXS characterization, we demonstrate that PML RING tetramerizes through highly conserved PML-specific sequences, which are required for NB assembly and PML sumoylation. Conserved residues implicated in RING dimerization of other TRIMs also contribute to PML tetramer stability. Wild-type PML rescues the ability of some RING mutants to form NBs as well as their sumoylation. Impaired RING tetramerization abolishes PML/RARA-driven leukemogenesis in vivo and arsenic-induced differentiation ex vivo. Our studies thus identify RING tetramerization as a key step in the NB macro-molecular scaffolding. They suggest that higher order RING interactions allow efficient UBC9 recruitment and thus change the biochemical nature of TRIM-facilitated post-translational modifications. äRING tetramerization is required for nuclear body biogenesis and PML s(epmc).pdf DeepDyve Pubget Overpricing