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"Semi-endogenous co-immunoprecipitation of SMN with intact or truncated Bap1 revealed that the ubiquitin C-terminal hydrolase domain of Bap1 is essential for the binding of Bap1 to SMN (Supplemental Figure 7F)."

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"Taken together, we concluded that Bap1 directly binds SMN and prevents SMN degradation by posttranslational deubiquitination of SMN.Since a lysine residue is one of the predominant targets for ubiquitination, we examined which of the lysine residues in SMN is critical for its ubiquitin-dependent degradation by introducing a non-lysine mutation on phylogenetically conserved lysine residues (Supplemental Figure 8A)."

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"These results indicate that Bap1 posttranscriptionally regulates SMN levels and thus affects the function of SMN in FAPs.To test the direct interaction between Bap1 and SMN, we performed endogenous reciprocal immunoprecipitation experiments using freshly isolated FAPs and revealed that Bap1 directly binds SMN in FAPs (Figure 7C)."