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• W2080548206 abstract "TLS (Translocated in LipoSarcoma), also termed FUS, is a multifunctional protein implicated in diverse cellular events such as maintaining genome integrity and regulating gene expression. We have focused on the role of TLS as a coregulator in transcriptional regulation. In the process of investigating TLS-binding proteins, we found that PRMT1 (protein arginine methyltransferase 1) was in complex with TLS. We analyzed the methylation status of endogenous TLS and demonstrated that TLS was arginine-methylated by PRMT1. Using mass spectrometry, we identified that four arginine residues within TLS (R216, R218, R242 and R394) were consistently dimethylated. We performed luciferase reporter assays to assess the functional consequence of TLS arginine methylation in transcriptional regulation and, interestingly, observed that TLS and PRMT1 synergistically coactivated transcription at the survivin promoter. Further analysis using a catalytic-dead PRMT1 or methylation inhibitor both showed that the synergistic transcriptional activation was mediated by TLS arginine-methylation. These results revealed a cooperative role of TLS and PRMT1 in transcriptional regulation." @default.
• W2080548206 created "2016-06-24" @default.
• W2080548206 creator A5010521586 @default.
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• W2080548206 creator A5038212374 @default.
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• W2080548206 date "2011-01-01" @default.
• W2080548206 modified "2023-10-16" @default.
• W2080548206 title "TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation" @default.
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• W2080548206 doi "https://doi.org/10.1016/j.bbrc.2010.12.097" @default.
• W2080548206 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21187067" @default.
• W2080548206 hasPublicationYear "2011" @default.
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