A critical role for hepatic protein arginine methyltransferase 1 isoform 2 in glycemic control.

ABSTRACT: Appropriate control of hepatic gluconeogenesis is essential for the organismal survival upon prolonged fasting and maintaining systemic homeostasis under metabolic stress. Here, we show protein arginine methyltransferase 1 (PRMT1), a key enzyme that catalyzes the protein arginine methylation process, particularly the isoform encoded by Prmt1 variant 2 (PRMT1V2), is critical in regulating gluconeogenesis in the liver. Liver-specific deletion of Prmt1 reduced gluconeogenic capacity in cultured hepatocytes and in the liver. Prmt1v2 was expressed at a higher level compared to Prmt1v1 in hepatic tissue and cells. Gain-of-function of PRMT1V2 clearly activated the gluconeogenic program in hepatocytes via interactions with PGC1α, a key transcriptional coactivator regulating gluconeogenesis, enhanc

SUBMITTER: Ma Y 

PROVIDER: S-EPMC9800170 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature