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p(HGNC:PTEN,pmod(P,T,382)) -> bp(GO:"cell proliferation")
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BEL Framework Large Corpus Document
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Here we show that the tail is necessary for maintaining PTEN stability. However, deletion of the tail also results in an increase in activity as measured by the ability of PTEN to induce a G1 arrest or to induce the transcriptional activity of FKHR. Thus, deletion of the tail does not result in a loss of PTEN function because, while unstable, the resultant protein is more active. We further demonstrate that the tail is a site for PTEN phosphorylation and that phosphorylation of the tail regulates both PTEN stability and activity. Furthermore, the individual phosphorylation mutants with substitutions S380A, T382A, and T383A, but not S385A, were again more active in inducing a G1 arrest and in inducing FKHR transcriptional activation (Fig. 5B and C, right). Taken together, these data show that the increased activity associated with deletion of the tail is entirely mimicked by mutations within the A4 cluster, specifically S380, T382, or T383.
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2014-07-03T14:29:51.380+02:00
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