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dc.contributor.author이민식-
dc.contributor.author정만형-
dc.contributor.author이현우-
dc.contributor.author한현지-
dc.contributor.author고아람-
dc.contributor.authorHewitt SM-
dc.contributor.author김재훈-
dc.contributor.author전경희-
dc.contributor.author정준영-
dc.contributor.author이철주-
dc.contributor.author조한별-
dc.contributor.author송재환-
dc.date.accessioned2015-12-03T02:07:04Z-
dc.date.available2015-12-03T02:07:04Z-
dc.date.issued201507-
dc.identifier.citationVOL 6, 7769-
dc.identifier.issn20411723-
dc.identifier.other45107-
dc.identifier.urihttp://pubs.kist.re.kr/handle/201004/50540-
dc.description.abstractThe activity of the phosphatase and tensin homologue (PTEN) is known to be suppressed via post-translational modification. However, the mechanism and physiological significance by which post-translational modifications lead to PTEN suppression remain unclear. Here we demonstrate that PTEN destabilization is induced by EGFR-or oncogenic PI3K mutation-mediated AKT activation in cervical cancer. EGFR/PI3K/AKT-mediated ubiquitination and degradation of PTEN are dependent on the MKRN1 E3 ligase. These processes require the stabilization of MKRN1 via AKT-mediated phosphorylation. In cervical cancer patients with high levels of pAKT and MKRN1 expression, PTEN protein levels are low and correlate with a low 5-year survival rate. Taken together, our results demonstrate that PI3K/AKT signals enforce positive-feedback regulation by suppressing PTEN function.-
dc.publisherNature Communications-
dc.titlePI3K/AKT activation induces PTEN ubiquitination and destabilization accelerating tumourigenesis-
dc.typeArticle-
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