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Article

Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating.

American journal of physiology. Renal physiology - 1 Mar 2009

Moeller Hanne B, MacAulay Nanna, Knepper Mark A, Fenton Robert A

Abstract excerpt

Arginine vasopressin (AVP)-regulated phosphorylation of the water channel aquaporin-2 (AQP2) at serine 256 (S256) is essential for its accumulation in the apical plasma membrane of collecting duct principal cells. In this study, we examined the role of additional AVP-regulated phosphorylation sites in the COOH-terminal tail of AQP2 on protein function. When expressed in Xenopus laevis oocytes, prevention of AQP2...

Topics

Animals
Aquaporin 2
Blotting, Western
Cell Membrane
Immunohistochemistry
Ion Channel Gating
Mice
Mutation
Oocytes
Osmosis
Phosphorylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinases

Water

Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 19144687
DOI: 10.1152/ajprenal.90682.2008
PMCID: PMC2660196

Genes

AQP2
AVP

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating.PMID 19144687Read ↗

Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus.Semantic proximity Read ↗

Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells.Semantic proximity Read ↗

p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation.Semantic proximity Read ↗

Vasopressin increases S261 phosphorylation in AQP2-P262L, a mutant in recessive nephrogenic diabetes insipidus.Semantic proximity Read ↗

Ser-256 phosphorylation dynamics of Aquaporin 2 during maturation from the ER to the vesicular compartment in renal cells.Semantic proximity Read ↗

Characterization of the putative phosphorylation sites of the AQP2 C terminus and their role in AQP2 trafficking in LLC-PK1 cells.Semantic proximity Read ↗

Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.Semantic proximity Read ↗

Protein phosphatase 2C is responsible for VP-induced dephosphorylation of AQP2 serine 261.Semantic proximity Read ↗

Regulation of the water channel aquaporin-2 by posttranslational modificationSemantic proximity Read ↗

Missorting of the Aquaporin-2 mutant E258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of E258.Semantic proximity Read ↗

Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells.Semantic proximity Read ↗

Mutations in sixth transmembrane domain of AQP2 inhibit its translocation induced by vasopression.Semantic proximity Read ↗

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