6533b7d4fe1ef96bd1261c13
RESEARCH PRODUCT
false
subject
medicine.medical_specialtyMutationurogenital systemPoint mutationMutantAquaporinBiologymedicine.disease_causeNephrogenic diabetes insipidusmedicine.diseaseGeneral Biochemistry Genetics and Molecular BiologyCell biologyEndocrinologyAquaporin 2Internal medicineArginine vasopressin receptor 2medicineProtein oligomerizationdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-01-01 | FEBS Open Bio |