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- W2382486809 abstract "Objective To confirm the interaction betweem NLK and Smad4 and to explore the effect of NLK on the function of Smad4. Methods Co-immunoprecipitation and GST Pull-down were used to detect the interaction between NLK and Smad4. GST Pull-down was used to map the domain through which Smad4 interacts with NLK. Luciferase reporter gene assay was used to study the effect of NLK and NLK( KM),the NLK mutant lacking kinase activity,on the transcription activity of Smad4. In vivo phosphorylation assay was used to detect whether NLK phosphorylated Smad4 or not. Results The data of Co-immunoprecipitation and GST Pull-down showed that NLK interacted with Smad4 in vivo and in vitro. The result of GST Pull-down showed that Smad4 interacted with NLK via MH2 domain. The results of luciferase reporter gene assay indicated that both NLK and NLK( KM) inhibited the transcription activity of Smad4. The result of in vivo phosphorylation assay showed that NLK could not phosphorylate Smad4 in vivo. Conclusion NLK interacts with Smad4 and inhibits the transcription activity of Smad4 independent of the kinase activity of NLK. The mechanism through which NLK negatively regulates the transcription of Smad4 requires further research." @default.
- W2382486809 created "2016-06-24" @default.
- W2382486809 creator A5052793314 @default.
- W2382486809 date "2014-01-01" @default.
- W2382486809 modified "2023-09-24" @default.
- W2382486809 title "NLK inhibits the transcription activity of Smad4 independent of its kinase activity" @default.
- W2382486809 hasPublicationYear "2014" @default.
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