Magnesium-dependent-protein phosphatase 1B regulates the protein arginine methyltransferase 5 through the modulation of myosin phosphatase.

ABSTRACT: Dysregulation of the expression levels and the activity of kinases/phosphatases is an intrinsic hallmark of tumor transformation and progression, as either as a primary cause or consequence. The myosin phosphatase (MP)/protein arginine methyltransferase 5 (PRMT5)/histone (H4) pathway is an oncogenic signaling pathway downregulating the gene expression of tumor suppressors. However, the upstream regulators of the pathway are unknown. We show that the Mg²⁺-dependent protein phosphatase 1 B (PP2Cb or PPM1B) interacts and regulates MP through the MYPT1 regulatory subunit, and this interplay results in the inactivation of the tumorigenic pathway driven by PRMT5. The phospho-Thr696 inhibitory residues of the MYPT1 regulatory subunit of MP was dephosphorylated by PPM1B. The inhibition

SUBMITTER: Keller I 

PROVIDER: S-EPMC11786752 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature