Article
Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.
The Journal of biological chemistry - 1 Sept 2017
Roche Jennifer Virginia, Survery Sabeen, Kreida Stefan, Nesverova Veronika, Ampah-Korsah Henry, Gourdon Maria, Deen Peter M T, Törnroth-Horsefield Susanna
Abstract excerpt
The interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein LIP5 targets AQP2 to multivesicular bodies and facilitates lysosomal degradation. This interaction is part of a process that controls AQP2 apical membrane abundance in a vasopressin-dependent manner, allowing for urine volume adjustment. Vasopressin regulates phosphorylation at four sites...
Topics
- Allosteric Regulation
- Amino Acid Substitution
- Aquaporin 2
- Binding Sites
- Endosomal Sorting Complexes Required for Transport
- Gene Deletion
- Humans
- Models, Molecular
- Mutation
- Peptide Fragments
- Phosphorylation
- Pichia