Zhang R, Zhao J, Song Y, Wang X, Wang L, Xu J, Song C, Liu F

Background/Aims: To identify the regulator of nucleotide-binding oligomerization domain-containing protein 1 (NOD1) and its regulatory function. Methods and Results : We performed a yeast two-hybrid screening assay and identified the E3 ligase RNF34 as a candidate partner of NOD1. Using co-immunoprecipitation (co-IP) and glutathione S transferase (GST)-pull down assays, we ...

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further confirmed that RNF34 is associated with NOD1. Western blotting showed that RNF34 downregulated the stability of NOD1 and promoted its ubiquitination. Functional analysis demonstrated that RNF34 overexpression inhibited NOD1-dependent activation of nuclear factor-kappa B (NF-κB), whereas knockdown of RNF34 using small interfering RNA increased NF-κB activation following stimulation from NOD1 overexpression or transfection of γ-D-glutamyl-meso-diaminopimelic acid. Conclusion: These findings confirm that RNF34 is a negative regulator of the NOD1 pathway through direct interaction and ubiquitination of NOD1, and suggest a novel regulatory mechanism of NOD1. © 2014 S. Karger AG, Basel.

Date: Jun. 27, 2014

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