IndraLab

Statements


PRPF8 is ubiquitinated. 8 / 8
| 8

sparser
"Shortly afterwards, it was also demonstrated that the E3 ligase named Prp19 increases the affinity between the ubiquitinated Prp3 protein and Prp8, thus contributing to stabilization of the triple snRNP."
| PMC

sparser
"A model was proposed in which inhibition of Brr2 by the ubiquitinated Prp8 leads to spliceosome assembly and stabilization of the triple snRNP (U4/U6–U5)."
| PMC

sparser
"Finally, we show that the conserved splicing factor Prp8 is ubiquitinated within purified triple snRNPs."

sparser
"It was further demonstrated that Prp8 is ubiquitinated within the tri-snRNP ( xref )."

sparser
"Important questions that can be addressed using our minimal system include determining whether the Prp8-CTF also promotes Brr2-depending unwinding of U2 and U6, and whether helicase activity is inhibited by Prp8 ubiquitination."

sparser
"In addition to recent studies suggesting that ubiquitination of Prp8 regulates tri-snRNP disassembly, xref , xref there are other indications that ubiquitin or ubiquitin-like proteins (such as Sumo and Hub1) play additional roles in splicing."

sparser
"Prp8, a key RNA-binding splicing factor, is ubiquitylated to suppress the U4/U6 snRNAs unwinding activity of Brr2 helicase and promote spliceosome assembly."

sparser
"Staley and Sontheimer uncovered a regulatory mechanism, namely that the activity of Brr2 is negatively regulated by ubiquitination of Prp8 (ref. xref )."