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- W2316855024 abstract "The transcriptional repressor polyhomeotic (Ph) is part of the polycomb group (PcG). PcG proteins are responsible for repressing Hox genes, a set of transcription factors that determine segmental identification early in development. PcG proteins are highly conserved throughout evolution, and recent studies have identified that the human homologue polyhomeotic-like protein 3 (PHC3) plays a role in tumor suppression in osteosarcomas. In order to understand how PHC3 functions, we utilized a cellular system with Ph. In our study we found that Ph is phosphorylated at a Ser residue several positions before the SAM domain. This region is important for controlling Ph SAM polymerization raising the possibility that phosphorylation alters the polymeric state of Ph. Phosphorylation was detected only in wild-type Ph and a mutant intended to increase polymerization, but not on polymer deficient Ph mutants. Because Ph repressive ability is dependent on SAM polymerization, we hypothesize that phosphorylation could trigger SAM depolymerization and consequently induce a relaxed chromatin state. To this point, mutating the phosphorylated Ser to Ala produced a better transcriptional repressor than wild-type. These results point to a potential way of controlling Ph SAM polymerization where phosphorylation leads to depolymerization and a replication competent chromatin state. Upon completing replication, the original repressive epigenetic state could be inherited by the daughter cell through dephosphorylation and Ph repolymerization. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the Second AACR International Conference on Frontiers in Basic Cancer Research; 2011 Sep 14-18; San Francisco, CA. Philadelphia (PA): AACR; Cancer Res 2011;71(18 Suppl):Abstract nr C27." @default.
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- W2316855024 date "2011-09-15" @default.
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- W2316855024 title "Abstract C27: Phosphorylation of the polycomb group protein polyhomeotic (Ph) induces a relaxed chromatin state through depolymerization of the Ph SAM domain" @default.
- W2316855024 doi "https://doi.org/10.1158/1538-7445.fbcr11-c27" @default.
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