Structural highlights
FunctionSMD1_HUMAN May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. Publication Abstract from PubMedProtein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase responsible for the majority of cellular symmetric dimethyl-arginine marks. PRMT5 uses substrate adaptors such as pICln, RIOK1, and COPR5 to recruit and methylate a wide range of substrates. Although the substrate adaptors play important roles in substrate recognition, how they direct PRMT5 activity towards specific substrates remains incompletely understood. Using biochemistry and cryogenic electron microscopy, we show that these adaptors compete for the same binding site on PRMT5. We find that substrate adaptor and substrate complexes are bound to PRMT5 through two peptide motifs, enabling these adaptors to act as flexible tethering modules to enhance substrate methylation. Taken together, our results shed structural and mechanistic light on the PRMT5 substrate adaptor function and the biochemical nature of PRMT5 interactors. Substrate adaptors are flexible tethering modules that enhance substrate methylation by the arginine methyltransferase PRMT5.,Jin CY, Hunkeler M, Mulvaney KM, Sellers WR, Fischer ES J Biol Chem. 2025 Jan 8;301(2):108165. doi: 10.1016/j.jbc.2025.108165. PMID:39793893[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 14:54, 19 February 2025.