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• W3045757908 abstract "The protein arginine methyltransferase 6 (PRMT6) is a coregulator of gene expression by methylation of the histone H3 on arginine 2 (H3R2), H4R3 and H2AR3 [1,2]. PRMT6 is aberrantly expressed in various types of human cancer, and abnormal methylation in cancers caused by overexpression of PRMT6 is considered to correlate with poor recovery prognosis [3,4]. However, mechanisms that regulate PRMT6 protein stability in cells remain largely unknown. Here we identified that an orphan F-box protein, FBXO24, that binds to 270 to 275 amino acid residues of PRMT6 to cause polyubiquitination of lysine at position 369 of PRMT6, which mediates its degradation via the ubiquitin-proteasome pathway. Overexpression of FBXO24 or knockout of PRMT6 was found to inhibit cell proliferation, migration, and invasion in H1299 cells. PRMT6 K369R mutant became resistant to degradation. Overexpression of PRMT6 K369R caused cell cycle progression, resulting in cell proliferation. Thus, our data confirm that FBXO24 regulates cell proliferation by mediating ubiquitin-dependent proteasomal degradation of PRMT6. • FBXO24 mediates the degradation of PRMT6 via the ubiquitin-proteasome pathway. • PRMT6 K369R mutant is resistant to degradation. • FBXO24 docks on a VGGRF motif within PRMT6. • PRMT6 degradation leads to inhibition of proliferation, migration, and invasion of H1299 cells." @default.
• W3045757908 created "2020-08-03" @default.
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• W3045757908 date "2020-09-01" @default.
• W3045757908 modified "2023-10-16" @default.
• W3045757908 title "SCF-FBXO24 regulates cell proliferation by mediating ubiquitination and degradation of PRMT6" @default.
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• W3045757908 doi "https://doi.org/10.1016/j.bbrc.2020.06.007" @default.
• W3045757908 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32828318" @default.
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