The E3 ubiquitin ligase CHIP mediates ubiquitination and proteasomal degradation of PRMT5.

ABSTRACT: Protein arginine methyltransferase 5 (PRMT5) is an important member of the protein arginine methyltransferase family that regulates many cellular processes through epigenetic control of target gene expression. Because of its overexpression in a number of human cancers and its essential role in cell proliferation, transformation, and cell cycle progression, PRMT5 has been recently proposed to function as an oncoprotein in cancer cells. However, how its expression is regulated in cancer cells remains largely unknown. We have previously demonstrated that the transcription of PRMT5 can be negatively regulated by the PKC/c-Fos signaling pathway through modulating the transcription factor NF-Y in prostate cancer cells. In the present study, we demonstrated that PRMT5 undergoes polyubiquitination

SUBMITTER: Zhang HT 

PROVIDER: S-EPMC5397900 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature