PIMT/TGS1: An evolving metabolic molecular switch with conserved methyl transferase activity. Issue 8 (August 2022)

• Record Type: Journal Article
• Authors: Edwin, Rebecca Kristina; Challa, Nagalakshmi; Sharma, Rahul; Satyamoorthy, K.; Parsa, Kishore; Misra, Parimal
• Is Part Of: Drug discovery today. Volume 27:Issue 8(2022)
• Page Start: 2386
• Page End: 2393
• Publication Date: 2022-08
• Subjects: Metabolism -- PIMT -- TGS1 -- PPARγ -- PRIP -- Transcription regulation -- Co-activator -- Glucose metabolism -- Methyl transferase; hTGS1 Human trimethyl guanosine synthase 1 -- MAPK Mitogen-activated protein kinase -- Med1 Mediator subunit 1 -- MEF Mouse embryonic fibroblast -- MeS Metabolic syndrome -- PBP Peroxisome proliferator-activated receptor-binding protein -- PEPCK Phosphoenolpyruvate carboxykinase -- PKC Protein kinase C -- PIMT PRIP-interacting protein with methyl transferase domain -- PPAR Peroxisome proliferator-activated receptor -- PPRE Peroxisome proliferator response element -- PRIP PPAR-interacting protein -- snoRNA Small nucleolar RNA -- snRNA Small nuclear RNA -- RXR Retinoid X Receptor -- TGS Trimethyl guanosine synthase; Drugs -- Design -- Periodicals; Drugs -- Research -- Periodicals; 615.1
• DOI: 10.1016/j.drudis.2022.04.018
• Languages: English
• ISSNs: 1359-6446

Abstract

Highlights: PRIP-interacting protein with methyl transferase domain (PIMT) is a dual-acting protein-A post-transcriptional modifier and an RNA methyl transferase. PIMT functions as a link between HAT- and non-HAT-containing coactivator complexes. PIMT regulates hepatic gluconeogenesis and lipid metabolism in the skeletal muscle. Cardiac-specific PIMT –/– mice suffered from increased myocardial damage. PIMT controls post-transcriptional regulation of HIV-1 and human telomerase RNA biogenesis. Abstract : Transcriptional coactivators play a crucial role in regulating gene expression. PRIP interacting protein with methyl transferase domain (PIMT)/trimethyl guanosine synthase 1 (TGS1) is a co-activator interacting protein with an RNA methyl transferase domain. PIMT serves as a bridge between HAT and non-HAT coactivators and differentially modulates gene expression. Disruption of PIMT is embryonic lethal. PIMT regulates hepatic gluconeogenesis and TNF-α-induced insulin resistance in the skeletal muscle. As a methyl transferase, PIMT controls post-transcriptional regulation of HIV-1 and is essential for human telomerase RNA biogenesis. This review comprehensively describes the dual role of PIMT, which promises to be a putative target in metabolic disorders.