Abstract |
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 causes nephrogenic 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.
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Authors | Noreen Klein, Nadine Kümmerer, Dominika Hobernik, Dirk Schneider |
Journal | FEBS open bio
(FEBS Open Bio)
Vol. 5
Pg. 640-6
( 2015)
ISSN: 2211-5463 [Print] England |
PMID | 26442203
(Publication Type: Journal Article)
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