Evidence map›Paper›PMID 25420462›Full record

ArticleProteomics2015

Comparative phosphoproteomic analysis of mammalian glomeruli reveals conserved podocin C-terminal phosphorylation as a determinant of slit diaphragm complex architecture.

Markus M Rinschen, Caroline Pahmeyer, Trairak Pisitkun, Nicole Schnell, Xiongwu Wu, Martina Maaß, Malte P Bartram, Tobias Lamkemeyer, Bernhard Schermer, Thomas Benzing and 1 more

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Tripartite Separation of Glomerular Cell Types and Proteomes from Reporter-Free Mice.Journal of the American Society of Nephrology : JASN · 2021
    Article
  4. Review
  5. Article
  6. Review
  7. MOLECULAR DESIGN OF THE KIDNEY FILTRATION BARRIER.Transactions of the American Clinical and Climatological Association · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Proline-dependent and basophilic kinases phosphorylate human TRPC6 at serine 14 to control channel activity through increased membrane expression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  12. N-Degradomic Analysis Reveals a Proteolytic Network Processing the Podocyte Cytoskeleton.Journal of the American Society of Nephrology : JASN · 2017
    Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 3 countries.

Markus M RinschenDepartment II of Internal Medicine and Center for Molecular Medicine, University of Cologne, Cologne, Germany; Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany; Systems Biology of Ageing Cologne (Sybacol), University of Cologne, Cologne, Germany.
Caroline Pahmeyer
Trairak Pisitkun
Nicole Schnell
Xiongwu Wu
Martina Maaß
Malte P Bartram
Tobias Lamkemeyer
Bernhard Schermer
Thomas Benzing
Paul T Brinkkoetter
Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases · DEUniversity of Cologne · DEChulalongkorn University · THNational Institutes of Health · US

Funding

Three-dimensional Structures Of Biological MacromoleculesZIAHL001027 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$8.1M
Intramural NIH HHS Z99 HL999999Intramural NIH HHS ZIA HL001027
6 · The paper itself

Abstract

Glomerular biology is dependent on tightly controlled signal transduction networks that control phosphorylation of signaling proteins such as cytoskeletal regulators or slit diaphragm proteins of kidney podocytes. Cross-species comparison of phosphorylation events is a powerful mean to functionally prioritize and identify physiologically meaningful phosphorylation sites. Here, we present the result of phosphoproteomic analyses of cow and rat glomeruli to allow cross-species comparisons. We discovered several phosphorylation sites with potentially high biological relevance, e.g. tyrosine phosphorylation of the cytoskeletal regulator synaptopodin and the slit diaphragm protein neph-1 (Kirrel). Moreover, cross-species comparisons revealed conserved phosphorylation of the slit diaphragm protein nephrin on an acidic cluster at the intracellular terminus and conserved podocin phosphorylation on the very carboxyl terminus of the protein. We studied a highly conserved podocin phosphorylation site in greater detail and show that phosphorylation regulates affinity of the interaction with nephrin and CD2AP. Taken together, these results suggest that species comparisons of phosphoproteomic data may reveal regulatory principles in glomerular biology. All MS data have been deposited in the ProteomeXchange with identifier PXD001005 (http://proteomecentral.proteomexchange.org/dataset/PXD001005).

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsConserved SequenceHumansIntracellular Signaling Peptides and ProteinsKidney GlomerulusMembrane ProteinsMolecular Sequence DataPhosphoproteinsPhosphorylationProtein Structure, TertiaryProteomeProteomicsSpecies SpecificityIntracellular Signaling Peptides and ProteinsMembrane ProteinsNPHS2 proteinPhosphoproteinsProteomeAnimal proteomicsGlomerulusKidneyPhosphoproteomicsPodocinSlit diaphragm complex

Identifiers

PMID25420462
PMCPMC6512310
OpenAlexW2058194775

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.