PIMT/TGS1: An evolving metabolic molecular switch with conserved methyl transferase activity

Rebecca Kristina Edwin, Nagalakshmi Challa, Rahul Sharma, K. Satyamoorthy, Kishore Parsa, Parimal Misra

Research output: Contribution to journalReview articlepeer-review

1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)2386-2393
Number of pages8
JournalDrug Discovery Today
Issue number8
Publication statusPublished - 08-2022

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Drug Discovery


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