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10.1038/nature16475 http://scihub22266oqcxt.onion/10.1038/nature16475 C5384647!5384647!26735018     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nature 2016 ; 529 (7585): 172-7 Nephropedia Template TP {{tp|p=26735018|t=2016. An ID2-dependent mechanism for VHL inactivation in cancer |pdf=|usr=}}{{26735018}} gab.com Text An ID2-dependent mechanism for VHL inactivation in cancer JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=26735018 #FOAvip Mechanisms that maintain cancer stem cells are crucial to tumor progression. The ID2 protein underpins cancer hallmarks including the cancer stem cell state. HIF? transcription factors, most notably HIF2?, are expressed in and required for maintenance of cancer stem cells (CSCs). However, the pathways that are engaged by ID2 or drive HIF2? accumulation in CSCs have remained unclear. We report that DYRK1A and DYRK1B kinases phosphorylate ID2 on Threonine-27 (T27). Hypoxia down regulates this phosphorylation via inactivation of DYRK1, whose activity is stimulated in normoxia by the oxygen sensing prolyl hydroxylase PHD1. ID2 binds to the VHL ubiquitin ligase complex, displaces VHL-associated Cullin-2, and impairs HIF2? ubiquitylation and degradation. Phosphorylation of ID2-T27 by DYRK1 blocks ID2-VHL interaction and preserves HIF2? ubiquitylation. In glioblastoma ID2 positively modulates HIF2? activity. Conversely, elevated expression of DYRK1 phosphorylates ID2- T27, leading to HIF2? destabilization, loss of glioma stemness, inhibition of tumor growth, and a more favorable outcome for patients with glioblastoma. Twit Text FOAVip An ID2-dependent mechanism for VHL inactivation in cancer ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=26735018 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26735018 #FOAvip English Wikipedia <ref>{{Cite pmid|26735018}}</ref> An ID2-dependent mechanism for VHL inactivation in cancer #MMPMID26735018 Lee SB; Frattini V; Bansal M; Castano AM; Sherman D; Hutchinson K; Bruce JN; Califano A; Liu G; Cardozo T; Iavarone A; Lasorella A Nature 2016[Jan]; 529 (7585): 172-7 PMID26735018show ga Mechanisms that maintain cancer stem cells are crucial to tumor progression. The ID2 protein underpins cancer hallmarks including the cancer stem cell state. HIF? transcription factors, most notably HIF2?, are expressed in and required for maintenance of cancer stem cells (CSCs). However, the pathways that are engaged by ID2 or drive HIF2? accumulation in CSCs have remained unclear. We report that DYRK1A and DYRK1B kinases phosphorylate ID2 on Threonine-27 (T27). Hypoxia down regulates this phosphorylation via inactivation of DYRK1, whose activity is stimulated in normoxia by the oxygen sensing prolyl hydroxylase PHD1. ID2 binds to the VHL ubiquitin ligase complex, displaces VHL-associated Cullin-2, and impairs HIF2? ubiquitylation and degradation. Phosphorylation of ID2-T27 by DYRK1 blocks ID2-VHL interaction and preserves HIF2? ubiquitylation. In glioblastoma ID2 positively modulates HIF2? activity. Conversely, elevated expression of DYRK1 phosphorylates ID2- T27, leading to HIF2? destabilization, loss of glioma stemness, inhibition of tumor growth, and a more favorable outcome for patients with glioblastoma. äAn ID2-dependent mechanism for VHL inactivation in cancer (epmc).pdf DeepDyve Pubget Overpricing