期刊论文详细信息
BMC Research Notes
The nucleotide-binding oligomerization domain-containing protein 1 (NOD1) polymorphism S7N does not affect receptor function
Tom P Monie1  Sophie Mayle1 
[1] Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA, Cambridge, UK
关键词: Caspase activation domain (CARD);    Serine;    Pattern recognition receptor;    NLR;    RIG-I;    Phosphorylation;    Polymorphism;    SNP;    NOD2;    NOD1;   
Others  :  1134362
DOI  :  10.1186/1756-0500-7-124
 received in 2013-10-22, accepted in 2014-02-28,  发布年份 2014
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【 摘 要 】

Background

Activation and signal transduction in the Nucleotide binding, leucine-rich repeat containing receptor (NLR) family needs to be tightly regulated in order to control the inflammatory response to exogenous and endogenous danger signals. Phosphorylation is a common cellular mechanism of regulation that has recently been shown to be important in signalling in another family of cytoplasmic pattern recognition receptors, the RIG-I like receptors. In addition, single nucleotide polymorphisms can alter receptor activity, potentially leading to dysfunction and/or a predisposition to inflammatory barrier diseases.

Findings

We have computationally analysed the N-terminus of NOD1 and found seven theoretical phosphorylation sites in, or immediately before, the NOD1 Caspase Activation Domain (CARD). Two of these, serine 7 and tyrosine 49 are also found as rare polymorphisms in the African-American population and European-American populations respectively. Mutating serine 7 to either an aspartic acid or an asparagine to mimic the potential impact of phosphorylation or the polymorphism respectively did not affect the response of NOD1 to ligand-mediated NFκB signalling.

Conclusions

The NOD1 polymorphism S7N does not interfere with receptor function in response to ligand stimulation.

【 授权许可】

   
2014 Mayle and Monie; licensee BioMed Central Ltd.

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