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Article

Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells.

PloS one - 1 Jan 2012

Rice William L, Zhang Yan, Chen Ying, Matsuzaki Toshiyuki, Brown Dennis, Lu Hua A Jenny

Abstract excerpt

The kidney maintains water homeostasis by modulating aquaporin 2 (AQP2) on the plasma membrane of collecting duct principal cells in response to vasopressin (VP). VP mediated phosphorylation of AQP2 at serine 256 is critical for this effect. However, the role of phosphorylation of other serine residues in the AQP2 C-terminus is less well understood. Here, we examined the effect of phosphorylation of S256, S261...

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Identifiers

PMID: 22403603
DOI: 10.1371/journal.pone.0032843
PMCID: PMC3293519

Genes

AQP2

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells.PMID 22403603Read ↗

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 ↗

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

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

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

Acute hypertonicity alters aquaporin-2 trafficking and induces a MAPK-dependent accumulation at the plasma membrane of renal epithelial cells.Semantic proximity Read ↗

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

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

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

Trafficking-dependent phosphorylation of Kv1.2 regulates voltage-gated potassium channel cell surface expression.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 ↗

A phosphorylation-dependent export structure in ROMK (Kir 1.1) channel overrides an endoplasmic reticulum localization signal.Semantic proximity Read ↗

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