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- W63304639 abstract "Vasopressin regulates water homeostasis by phosphorylation Aquaporin-2 (AQP2) at S256 and translocating them from vesicles to the apical membrane. AQP2-E258K causes dominant Nephrogenic Diabetes Insipidus (NDI). To address the molecular mechanism for dominant NDI, AQP2-E258K was studied in polarized MDCK. AQP2-E258K mainly co-localized with the late endosomes(LE)/lysosomes(Lys). Upon co-expression, wild-type (wt) AQP2 interacted with AQP2-E258K and localized to LE/Lys, independent of forskolin stimulation, while wt-AQP2 alone translocated from vesicles to the apical membrane. Orthophosphate labeling revealed that forskolin increased phosphorylation of wt-AQP2 and AQP2-E258K, but not AQP2-S256A, indicating that the E258K mutation does not interfere with the AQP2-S256 phosphorylation. In contrast to wt-AQP2, but consistent with the introduced PKC consensus site, AQP2-E258K was phosphorylated by phorbol esters. Besides the 29 kDa band, however, a band of 38 kDa was observed for AQP2-E258K only, which, consistent with the mass increase, was mono-ubiquitinated AQP2-E258K. Mono-ubiquitination induces endocytosis of membrane proteins and targets them to LE/Lys. As the AQP2-E258K NDI patients show a shortened period of urine concentration following dDAVP administration compared to central DI patients, increased endocytoses and LE/Lys targeting of wt-AQP2/AQP2-E258K complexes due to AQP2-E258K mono-ubiquitination provides an explanation for dominant NDI in these patients." @default.
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- W63304639 date "2007-01-01" @default.
- W63304639 modified "2023-10-16" @default.
- W63304639 title "Missorting to late endosome/lysosomes due to increased phosphorylation by protein kinase C and mono‐ubiquitination of the Aquaporin‐2 mutant E258K might explain its role in dominant Nephrogenic Diabetes Insipidus" @default.
- W63304639 doi "https://doi.org/10.1096/fasebj.21.6.a956-a" @default.
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