PXD005488-1

PXD005488 is an original dataset announced via ProteomeXchange.

Title	Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct
Description	Phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. The phosphatases that dephosphorylate AQP2 have not been identified. Here, we use large-scale data integration techniques to identify serine-threonine phosphatases likely to interact with AQP2 in renal collecting duct principal cells. As a first step, we have created a comprehensive list of 38 S/T phosphatase catalytic subunits present in the mammalian genome. Then we used Bayes’ theorem to integrate available information from large-scale data sets from proteomic and transcriptomic studies in order to rank the known S/T phosphatases with regard to the likelihood that they interact with AQP2 in renal collecting duct cells. To broaden the analysis, we have generated new proteomic data (LC-MS/MS) identifying 4538 distinct proteins including 22 S/T phosphatases in cytoplasmic fractions from native inner medullary collecting duct cells from rats. The official gene symbols corresponding to the top-ranked phosphatases (common names in parentheses) were: Ppp1cb (PP1-beta), Ppm1g (PP2C), Ppp1ca (PP1-alpha), Ppp3ca (PP2-B or calcineurin), Ppp2ca (PP2A-alpha), Ppp1cc (PP1-gamma), Ppp2cb (PP2A-beta), Ppp6c (PP6C) and Ppp5c (PP5). This ranking correlates well with results of prior reductionist studies of ion and water channels in renal collecting duct cells.
HostingRepository	PRIDE
AnnounceDate	2018-10-26
AnnouncementXML	Submission_2018-10-26_12:28:38.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Chung-Lin Chou
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2016-12-02 02:12:37	ID requested
⏵ 1	2018-10-26 12:28:40	announced
2	2024-10-22 04:34:09	announced	2024-10-22: Updated project metadata.

LeMaire SM, Raghuram V, Grady CR, Pickering CM, Chou CL, Umejiego EN, Knepper MA, Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct. Am J Physiol Renal Physiol, 312(1):F84-F95(2017) [pubmed]

curator keyword: Biological

submitter keyword: systems biology

collecting duct

kidney

vasopressin

LC-MS/MS

Mark A. Knepper
contact affiliation	Epithelial Systems Biology Laboratory, National Heart, Lung, and Blood Institute, National Institutes of Health
contact email	knepperm@nhlbi.nih.gov
lab head
Chung-Lin Chou
contact affiliation	National Institutes of Health
contact email	chouj@nhlbi.nih.gov
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD005488
     1. Label: PRIDE project
     2. Name: Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct