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PRPF8 inhibits SNRNP200. 7 / 7
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"A C-terminal fragment of Prp8 was shown to inhibit Brr2 ATPase activity in vitro [ 35 ]."
22464735
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"Given the mechanistic analogy between histone mRNA processing and splicing, we thus envisage that SLBP ubiquitylation may suppress hPrp43 helicase activity in histone mRNA processing similar to Prp8 u[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
27203182
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"These proteins show multiple strong genetic (Kuhn et al. 2002; Bottner et al. 2005; Grainger and Beggs 2005; Liu et al. 2006), yeast-two-hybrid (van Nues and Beggs 2001), and physical interactions (Achsel et al. 1998), indicating a high degree of coordination between them.Initial genetic evidence indicated that the Prp8 C-terminal Jab1/MPN domain negatively regulated Brr2 unwinding during splicing (Kuhn and Brow 2000; Kuhn et al. 2002)."
26968627
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"Thus Prp8-RP mutations provide a potent tool to understand how deregulation of Brr2 by Prp8 impacts splicing.Here we present evidence that Prp8-RP mutants deregulate Brr2 activity both in vitro and in vivo."
26968627
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"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)."
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"In humans, phosphorylation of Prp6 that occurs after the tri-snRNP being integrated into the B-complex may release the inhibition of Brr2 by Prp8 and is important for spliceosomal B-complex activation [ xref , xref ]."
27058959
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"The RNase H domain of PRPF8 inhibits loading of SNRNP200 to U4 snRNA, and a C-terminal part of PRPF8 modulates the SNRNP200 activity for the unwinding of U4/U6 snRNA duplex XREF_BIBR - XREF_BIBR."
25450007