Evidence map›Paper›PMID 21209370›Full record

ArticleAmerican journal of physiology. Cell physiology2011

Large-scale phosphoproteomic analysis of membrane proteins in renal proximal and distal tubule.

Marina Feric, Boyang Zhao, Jason D Hoffert, Trairak Pisitkun, Mark A Knepper

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

  1. Article
  2. Inactivation mechanisms of NaCommunications biology · 2025
    Article
  3. Review
  4. The role ofJournal of pharmaceutical analysis · 2023
    Review
  5. Review
  6. SGLT2 inhibition effect on salt-induced hypertension, RAAS, and NaAmerican journal of physiology. Renal physiology · 2022
    Article
  7. Article
  8. Hydrogen peroxide (HScientific reports · 2021
    Article
  9. Article
  10. Molecular regulation of NKCC2 in blood pressure control and hypertension.Current opinion in nephrology and hypertension · 2019
    Review
  11. Review
  12. NaPi-IIa interacting partners and their (un)known functional roles.Pflugers Archiv : European journal of physiology · 2019
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Sodium-glucose cotransport.Current opinion in nephrology and hypertension · 2015
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Marina FericEpithelial Systems Biology Laboratory, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA.
Boyang Zhao
Jason D Hoffert
Trairak Pisitkun
Mark A Knepper

Funding

Solute And Water Transport In Renal EpitheliaZIAHL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2009 to 2025
$34.9M
Computational Tools for ProteomicsZIAHL006129 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2025
$8.1M
SOLUTE AND WATER TRANSPORT IN RENAL EPITHELIAZ01HL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK A · 1998 to 2008
$3.8M
Urinary ExosomesZIAHL006128 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2019
$354k
NHLBI NIH HHS Z01-HL-001285
6 · The paper itself

Abstract

Recent advances in mass spectrometry (MS) have provided means for large-scale phosphoproteomic profiling of specific tissues. Here, we report results from large-scale tandem MS [liquid chromatography (LC)-MS/MS]-based phosphoproteomic profiling of biochemically isolated membranes from the renal cortex, with focus on transporters and regulatory proteins. Data sets were filtered (by target-decoy analysis) to limit false-positive identifications to <2%. A total of 7,125 unique nonphosphorylated and 743 unique phosphorylated peptides were identified. Among the phosphopeptides identified were sites on transporter proteins, i.e., solute carrier (Slc, n = 63), ATP-binding cassette (Abc, n = 4), and aquaporin (Aqp, n = 3) family proteins. Database searches reveal that a majority of the phosphorylation sites identified in transporter proteins were previously unreported. Most of the Slc family proteins are apical or basolateral transporters expressed in proximal tubule cells, including proteins known to mediate transport of glucose, amino acids, organic ions, and inorganic ions. In addition, we identified potentially important phosphorylation sites for transport proteins from distal nephron segments, including the bumetanide-sensitive Na-K-2Cl cotransporter (Slc12a1 or NKCC2) at Ser(87), Thr(101), and Ser(126) and the thiazide-sensitive Na-Cl cotransporter (Slc12a3 or NCC) at Ser(71) and Ser(124). A subset of phosphorylation sites in regulatory proteins coincided with known functional motifs, suggesting specific regulatory roles. An online database from this study (http://dir.nhlbi.nih.gov/papers/lkem/rcmpd/) provides a resource for future studies of transporter regulation.

Indexed as

Amino Acid SequenceAnimalsChromatography, LiquidHumansKidney Tubules, DistalKidney Tubules, ProximalMaleMembrane ProteinsMolecular Sequence DataPhosphopeptidesPhosphoproteinsProtein ConformationProtein Structure, TertiaryProteomeRatsRats, Sprague-DawleyMembrane ProteinsPhosphopeptidesPhosphoproteinsProteome

Identifiers

PMID21209370
PMCPMC3074622

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.