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10.1016/j.molcel.2016.10.012 http://scihub22266oqcxt.onion/10.1016/j.molcel.2016.10.012 C5123859!5123859!27840026     free     free     free       Mol+Cell 2016 ; 64 (4): 774-89 Nephropedia Template TP {{tp|p=27840026|t=2016. CRY2 and FBXL3 cooperatively degrade c-MYC |pdf=|usr=}}{{27840026}} gab.com Text CRY2 and FBXL3 cooperatively degrade c-MYC JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27840026 #FOAvip For many years, a connection between circadian clocks and cancer has been postulated. Here, we describe an unexpected function for the circadian repressor CRY2 as a component of an FBXL3-containing E3 ligase that recruits T58-phosphorylated c-MYC for ubiquitylation. c-MYC is a critical regulator of cell proliferation; T58 is central in a phosphodegron long recognized as a hotspot for mutation in cancer. This site is also targeted by FBXW7, though the full machinery responsible for its turnover has remained obscure. CRY1 cannot substitute for CRY2 in promoting c-MYC degradation; their unique functions may explain prior conflicting reports that have fueled uncertainty about the relationship between clocks and cancer. Thus, we demonstrate that c-MYC is a target of CRY2-dependent protein turnover, suggesting a molecular mechanism for circadian control of cell growth and a new paradigm for circadian protein degradation. Twit Text FOAVip CRY2 and FBXL3 cooperatively degrade c-MYC ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27840026 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27840026 #FOAvip English Wikipedia <ref>{{Cite pmid|27840026}}</ref> CRY2 and FBXL3 cooperatively degrade c-MYC #MMPMID27840026 Huber AL; Papp SJ; Chan AB; Henriksson E; Jordan SD; Kriebs A; Nguyen M; Wallace M; Li Z; Metallo CM; Lamia KA Mol Cell 2016[Nov]; 64 (4): 774-89 PMID27840026show ga For many years, a connection between circadian clocks and cancer has been postulated. Here, we describe an unexpected function for the circadian repressor CRY2 as a component of an FBXL3-containing E3 ligase that recruits T58-phosphorylated c-MYC for ubiquitylation. c-MYC is a critical regulator of cell proliferation; T58 is central in a phosphodegron long recognized as a hotspot for mutation in cancer. This site is also targeted by FBXW7, though the full machinery responsible for its turnover has remained obscure. CRY1 cannot substitute for CRY2 in promoting c-MYC degradation; their unique functions may explain prior conflicting reports that have fueled uncertainty about the relationship between clocks and cancer. Thus, we demonstrate that c-MYC is a target of CRY2-dependent protein turnover, suggesting a molecular mechanism for circadian control of cell growth and a new paradigm for circadian protein degradation. äCRY2 and FBXL3 cooperatively degrade c-MYC (epmc).pdf DeepDyve Pubget Overpricing