ArticleThe Journal of biological chemistry2017
PRMT5 C-terminal Phosphorylation Modulates a 14-3-3/PDZ Interaction Switch.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Therapeutic targeting of chromatin alterations in leukemia and solid tumors.International journal of cancer · 2026Review
- Arginine methylation in cancer: mechanisms and therapeutic implications.Biomarker research · 2025Review
- Article
- PRMT5-mediated regulatory arginine methylation of RIPK3.Cell death discovery · 2023Article
- Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023Review
- Nitric Oxide Implication in Potato Immunity toInternational journal of molecular sciences · 2022Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- The Structure and Functions of PRMT5 in Human Diseases.Life (Basel, Switzerland) · 2021Review
- Human papillomavirus E6 and E7: What remains?Tumour virus research · 2021Review
- Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms.Nature communications · 2021Article
- The PDZ Domain Protein SYNJ2BP Regulates GRK-Dependent Sst2A Phosphorylation and Downstream MAPK Signaling.Endocrinology · 2021Article
- Systematic Analysis of the Impact of R-Methylation on RBPs-RNA Interactions: A Proteomic Approach.Frontiers in molecular biosciences · 2021Article
- Novel phospho-switch function of delta-catenin in dendrite development.The Journal of cell biology · 2020Article
- Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14-3-3 proteins in vitro.Scientific reports · 2020Article
- Modulating the modulators: regulation of protein arginine methyltransferases by post-translational modifications.Drug discovery today · 2020Review
- PRMT5 function and targeting in cancer.Cell stress · 2020Review
- Regulation of a PRMT5/NF-κB Axis by Phosphorylation of PRMT5 at Serine 15 in Colorectal Cancer.International journal of molecular sciences · 2020Article
- The regulation, functions and clinical relevance of arginine methylation.Nature reviews. Molecular cell biology · 2019Review
- LKB1 regulates PRMT5 activity in breast cancer.International journal of cancer · 2019Article
- Proteome-wide analysis of phospho-regulated PDZ domain interactions.Molecular systems biology · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
PRMT5 is the primary enzyme responsible for the deposition of the symmetric dimethylarginine in mammalian cells. In an effort to understand how PRMT5 is regulated, we identified a threonine phosphorylation site within a C-terminal tail motif, which is targeted by the Akt/serum- and glucocorticoid-inducible kinases. While investigating the function of this posttranslational modification, we serendipitously discovered that its free C-terminal tail binds PDZ domains (when unphosphorylated) and 14-3-3 proteins (when phosphorylated). In essence, a phosphorylation event within the last few residues of the C-terminal tail generates a posttranslational modification-dependent PDZ/14-3-3 interaction "switch." The C-terminal motif of PRMT5 is required for plasma membrane association, and loss of this switching capacity is not compatible with life. This signaling phenomenon was recently reported for the HPV E6 oncoprotein but has not yet been observed for mammalian proteins. To investigate the prevalence of PDZ/14-3-3 switching in signal transduction, we built a protein domain microarray that harbors PDZ domains and 14-3-3 proteins. We have used this microarray to interrogate the C-terminal tails of a small group of candidate proteins and identified ERBB4, PGHS2, and IRK1 (as well as E6 and PRMT5) as conforming to this signaling mode, suggesting that PDZ/14-3-3 switching may be a broad biological paradigm.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.