Evidence map›Paper›PMID 20664558›Full record

ArticleKidney international2010

Proteomic analysis of the slit diaphragm complex: CLIC5 is a protein critical for podocyte morphology and function.

Brian A Pierchala, Maura R Muñoz, Cynthia C Tsui

Open access · greenAbstract read
In one paragraph

Article in Kidney international, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

42 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Renal cell markers: lighthouses for managing renal diseases.American journal of physiology. Renal physiology · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Dysregulated Dynein-Mediated Trafficking of Nephrin Causes INF2-related Podocytopathy.Journal of the American Society of Nephrology : JASN · 2021
    Article
  14. Review
  15. Article
  16. Long-Tailed Unconventional Class I Myosins in Health and Disease.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Brian A PierchalaDepartment of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
Maura R Muñoz
Cynthia C Tsui
Michigan Medicine · USUniversity of Michigan–Ann Arbor · US

Funding

University of Michigan O'Brien Kidney Translational Core CenterP30DK081943 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KRETZLER, MATTHIAS · 2008 to 2022
$12.9M
Survival and growth-promotion mechanisms of the GDNF family ligands (GFLs)R01NS058510 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PIERCHALA, BRIAN ANTHONY · 2008 to 2012
$1.7M
GDNF and Ret are critical for glomerular development, maintenance, and protectionK08DK084210 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSUI, CYNTHIA · 2009 to 2013
$777k
NIDDK NIH HHS K08 DK084210NIDDK NIH HHS P30 DK081943NIDDK NIH HHS P30DK081943NINDS NIH HHS R01 NS058510NINDS NIH HHS R01NS058510
6 · The paper itself

Abstract

Podocytes are morphologically complex cells, the junctions of which form critical elements of the final filtration barrier. Disruption of their foot processes and slit diaphragms occur early in the development of many glomerular diseases. Here, we biochemically purified fractions enriched with slit diaphragm proteins and performed a proteomic analysis to identify new components of this important structure. Several known slit diaphragm proteins were found, such as podocin and nephrin, confirming the validity of the purification scheme. However, proteins on the apical membrane such as podocalyxin were neither enriched nor identified in our analysis. The chloride intracellular channel protein 5 (CLIC5), predominantly expressed in podocytes, was enriched in these fractions and localized in the foot process apical and basal membranes. CLIC5 colocalized and associated with the ezrin/radixin/moesin complex and with podocalyxin in podocytes in vivo. It is important to note that CLIC5(-/-) mice were found to have significantly decreased foot process length, widespread foot process abnormalities, and developed proteinuria. The ezrin/radixin/moesin complex and podocalyxin were significantly decreased in podocytes from CLIC5(-/-) mice. Thus, our study identifies CLIC5 as a new component that is enriched in and necessary for foot process integrity and podocyte function in vivo.

Indexed as

Cell ShapeProteomicsAnimalsCell MembraneCells, CulturedChloride ChannelsCytoskeletal ProteinsEzrinHumansMembrane ProteinsMiceMice, KnockoutMicrofilament ProteinsMultiprotein ComplexesPermeabilityPodocytesChloride ChannelsCLIC5 protein, mouseCytoskeletal ProteinsEzrinMembrane ProteinsMicrofilament ProteinsmoesinMultiprotein Complexespodocan protein, mouseProteinsradixin

Identifiers

PMID20664558
PMCPMC5538030
OpenAlexW2043807258

What OpenQuestion holds

Textmetadata
LicenceTDM
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.