The AQP2 mutation V71M causesnephrogenic diabetes insipidus in humans but does not impair the function of a bacterial homolog

FEBS Open Bio

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关键词: GlpF;    Aquaporin;    Nephrogenic diabetes insipidus;    Activity;    Protein oligomerization;   

DOI  :  10.1016/j.fob.2015.07.003

来源: publisher

【 摘 要 】

Several point mutations have been identified in human aquaporins, but their effects on the function of the respective aquaporins are mostly enigmatic. We analyzed the impact of the aquaporin 2 mutation V71M, which causesnephrogenic diabetes insipidus in humans, on aquaporin structure and activity, using the bacterial aquaglyceroporin GlpF as a model. Importantly, the sequence and structure around the V71M mutation is highly conserved between aquaporin 2 and GlpF. The V71M mutation neither impairs substrate flux nor oligomerization of the aquaglyceroporin. Therefore, the human aquaporin 2 mutant V71M is most likely active, but cellular trafficking is probably impaired.

【 授权许可】

Unknown