TY - JOUR
T1 - PIMT/TGS1
T2 - An evolving metabolic molecular switch with conserved methyl transferase activity
AU - Edwin, Rebecca Kristina
AU - Challa, Nagalakshmi
AU - Sharma, Rahul
AU - Satyamoorthy, K.
AU - Parsa, Kishore
AU - Misra, Parimal
N1 - Funding Information:
This review was supported by a grant awarded by the Indian Department of Biotechnology (DBT) (# BT/PR32804/MED/30/2138/2019). The authors thank G. Sujeevan Reddy for help with drawing the (inset) structure in Fig. 1 in ChemDraw. Figs. 2, 3 and 4 were created using BioRender.com .
Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2022/8
Y1 - 2022/8
N2 - 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.
AB - 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.
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U2 - 10.1016/j.drudis.2022.04.018
DO - 10.1016/j.drudis.2022.04.018
M3 - Review article
C2 - 35462043
AN - SCOPUS:85132140971
SN - 1359-6446
VL - 27
SP - 2386
EP - 2393
JO - Drug Discovery Today
JF - Drug Discovery Today
IS - 8
ER -
