Proteomics

Dataset Information

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Signaling Pathways in Vasopressin-Mediated Regulation of Aquaporin-2

ABSTRACT: Vasopressin controls water excretion by regulating the water channel protein, aquaporin 2. Vasopressin acts in the renal collecting duct by binding to a G-protein coupled receptor and activating protein kinase A (PKA). Signaling events beyond PKA are largely unknown. Ultra-deep phosphoproteomic analysis of collecting duct cells isolated from rat kidneys identified and quantified 10,738 phosphorylation sites. Vasopressin significantly altered the abundance of only 219 of these phosphorylation sites, suggesting a highly selective effect on cell signaling. The regulated sites were mapped to cellular processes shown in prior studies to be involved in aquaporin-2 regulation. The mapping and full data set was used to create an online data resource to guide future studies.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Epithelial Cell, Kidney

SUBMITTER: CHIN-RANG YANG  

LAB HEAD: Mark Knepper

PROVIDER: PXD011245 | Pride | 2020-05-25

REPOSITORIES: pride

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Dataset's files

Source:
Action DRS
IP_Fe.raw Raw
IP_Fe_Ti_Mascot.msf Msf
IP_Fe_Ti_Sequest.msf Msf
IP_Ti.raw Raw
UB_01-12_Mascot.msf Msf
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Publications

Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct.

Deshpande Venkatesh V   Kao Anika A   Raghuram Viswanathan V   Datta Arnab A   Chou Chung-Lin CL   Knepper Mark A MA  

American journal of physiology. Renal physiology 20190717 4

Vasopressin controls water balance largely through PKA-dependent effects to regulate the collecting duct water channel aquaporin-2 (AQP2). Although considerable information has accrued regarding the regulation of water and solute transport in collecting duct cells, information is sparse regarding the signaling connections between PKA and transport responses. Here, we exploited recent advancements in protein mass spectrometry to perform a comprehensive, multiple-replicate analysis of changes in t  ...[more]

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