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Target intelligence / Profile preview
Protein Arginine Methyltransferase 5–Methylthioadenosine Complex (PRMT5-MTA)
- Target
- PRMT5-MTA
- Molecular classification
- Enzyme Complex, Histone Modification, Protein Methyltransferase, Arginine Methyltransferase
01
Overview
The Protein Arginine Methyltransferase 5–Methylthioadenosine (PRMT5-MTA) complex refers to the functional interaction between PRMT5, a type II arginine methyltransferase enzyme, and its cofactor or modulator, MTA. PRMT5 catalyzes the symmetric dimethylation of arginine residues on both histone and non-histone proteins, playing key roles in chromatin regulation, gene expression, RNA splicing, and DNA repair. In MTAP-deleted cancers, elevated levels of MTA bind to PRMT5, creating a unique vulnerability that can be exploited by inhibitors specifically targeting the PRMT5–MTA complex.
- Other names
- PRMT5-MTA Complex
02
Mechanism of action
Selective inhibition of PRMT5-MTA complex
03
Biological functions
Gene silencingRNA splicingDNA repairChromatin regulationEpigenetic regulation
04
Disease associations
CancerMTAP-deleted tumors
05
Safety considerations
On-target toxicityResistance mechanisms
06
Interacting drugs
MRTX1719
07
Biomarkers
MTAP deletionMTA levels
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