[HTML][HTML] RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and …
G Guderian, C Peter, J Wiesner, A Sickmann… - Journal of Biological …, 2011 - ASBMB
Protein arginine methylation plays a critical role in differential gene expression through
modulating protein-protein and protein-DNA/RNA interactions. Although numerous proteins
undergo arginine methylation, only limited information is available on how protein arginine
methyltransferases (PRMTs) identify their substrates. The human PRMT5 complex consists
of PRMT5, WD45/MEP50 (WD repeat domain 45/methylosome protein 50), and pICln and
catalyzes the symmetrical arginine dimethylation of its substrate proteins. pICln recruits the …
modulating protein-protein and protein-DNA/RNA interactions. Although numerous proteins
undergo arginine methylation, only limited information is available on how protein arginine
methyltransferases (PRMTs) identify their substrates. The human PRMT5 complex consists
of PRMT5, WD45/MEP50 (WD repeat domain 45/methylosome protein 50), and pICln and
catalyzes the symmetrical arginine dimethylation of its substrate proteins. pICln recruits the …