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AAR2 binds PRPF8. 39 / 39
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"PRPF8 binding to R2TP and AAR2 chaperones was increased in the absence of PIH1D1, suggesting that the formation of the R2TP complex through PIH1D1 binding is important for the release of PRPF8 from R2TP and AAR2 [59]."
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"Despite the biochemical and structural evidence reported previously, which supports this switch, a caveat of our AAR2–PRPF8 RH structure may be that the RH β-finger module makes crystal contacts with a neighboring symmetry-related RH β-finger module."
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"In contrast, our observations of (i) human AAR2 failing to sequester the PRPF8 JM domain from SNRNP200 395–2136 and (ii) AAR2 concomitantly binding to a PRPF8 fragment encompassing the RH and JM domains and SNRNP200 395–2136 suggest that an equivalent, long-lived intermediate is not formed in the human system."
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"CK2α1 and SGK2 kinases can abrogate the interaction between the spliceosomal proteins AAR2 and PRPF8, and NEK6 kinase was found to mediate the estrogen receptor (ERα) interaction with 14-3-3 proteins."
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"In the cytoplasm, PRPF8 forms a complex with AAR2, a protein required for the assembling of U5 snRNP that is replaced by the SNRNP200 helicase after PRPF8 is transported from the cytoplasm to the nucleus ( xref , xref )."
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"Nevertheless, the GFP-AAR2 IP purified only a few other U5 proteins, which is in agreement with the idea that AAR2 binds PRPF8 mostly before its association with U5 snRNA."
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"The results showed that the interactions of PRPF8 with R2TP and AAR2 increased in the absence of PIH1D1."
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"Aar2 also binds the Prp8 α-finger, which is bent at a conserved Proline (yeast Pro1602, human Pro1530; Extended Data Fig. 5b)."
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"In the cytoplasm, PRPF8 forms a complex with AAR2, a protein required for the assembling of U5 snRNP that is replaced by the SNRNP200 helicase after PRPF8 is transported from the cytoplasm to the nucleus (1,2)."
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"ZNHIT2, ECD, AAR2 and PRPF8 can form complexes with R2TP."
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"The crystal structure of human AAR2 bound to the central spliceosomal factor PRPF8 and in vitro functional data yield insights into the structural basis of snRNP assembly in humans."
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"Based on the structure of the AAR2–PRPF8 RH complex, the importance of the interacting regions and residues was probed and AAR2 variants were designed that failed to stably bind PRPF8 in vitro ."
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"In contrast to the situation in yeast, we find that a human AAR2–PRPF8 RH complex does not bind the PRPF8 JM domain and thus permits the formation of a trimeric AAR2–PRPF8–SNRNP200 complex."
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"As in yeast, the human AAR2–PRPF8 RH interaction is abrogated in vitro by a phosphomimetic S284E (S253E in yeast) mutation, indicating highly conserved regulation of AAR2 by phosphorylation."
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"Our results shed the first light on the human AAR2–PRPF8 RH interface and imply a different role of AAR2 in spliceosomal assembly than in yeast."
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"Crystal structure of a human AAR2 Δloop –PRPF8 RH complex."
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"Here, we report the crystal structure of the human AAR2 Δloop –PRPF8 RH complex at 2.35 Å resolution."
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"In contrast to the situation in yeast, we find that a human AAR2–PRPF8 complex does not bind the PRPF8 JM domain and thus permits the formation of a trimeric AAR2–PRPF8–SNRNP200 complex."
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"Nevertheless, the GFP-AAR2 IP purified only a few other U5 proteins, which is in agreement with the idea that AAR2 binds PRPF8 mostly before its association with U5 snRNA."
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"Despite the low sequence identity, the overall structure of human AAR2 Δloop in the AAR2 Δloop –PRPF8 RH complex is very similar to that of yeast Aar2p Δloop in complex with the Prp8p RH and JM domains (Weber et al. , 2013 xref ; Galej et al. , 2013 xref ; root-mean-square deviation of 2.13 Å for 236 pairs from 330 AAR2 and 342 Aar2p C α atoms;)."
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"To this end, we investigated the binding of WT AAR2 to WT PRPF8 RH in previous work, which is only shown here for comparison (Figs."
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"Here, we report the crystal structure of the human AAR2 –PRPF8 complex at 2."
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"Residues 65–71 of AAR2 and residues 2001–2008 of PRPF8 were modeled with low confidence due to weaker electron density.Despite the low sequence identity, the overall structure of human AAR2 in the AAR2 –PRPF8 complex is very similar to that of yeast Aar2p in complex with the Prp8p RH and JM domains (Weber et al., 2013 ▸; Galej et al., 2013 ▸; root-mean-square deviation of 2."
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"Indeed, also confirming a prior study (Malinová et al. , 2017 xref ), AAR2–PRPF8 RH did not stably bind PRPF8 JM in analytical SEC (Figs."
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"The interactions with the RH domain described here in the Prp8/Aar2 complex, the B complex (with Snu 66), the C* complex (with the branch duplex RNA), and the intron lariat spliceosome (with Cwf19) es[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"To test whether AAR2 is likely to prevent a switch of PRPF8 into the step 2 conformation, we explored whether AAR2 binds a PRPF8 variant that is stabilized in the step 2 conformation (T1789P; Schellenberg et al., 2013 ▸)."
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"Instead, a stable AAR2–PRPF8 RM-JM –SNRNP200 395–2136 ternary complex was formed upon mixing the components (Fig. 3 xref b )."
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"Yeast and human PRPF8 associate with the chaperone AAR2, which helps to properly fold PRPF8 xref – xref ."
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