Evidence map›Paper›PMID 11457882›Full record

ArticleThe Journal of clinical investigation2001

Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton.

T Takeda, T McQuistan, R A Orlando, M G Farquhar

Open access · greenAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 259 citations in OpenAlex.

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  20. Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS.Journal of the American Society of Nephrology : JASN · 2019
    Article

59 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

T TakedaDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California, USA.
T McQuistan
R A Orlando
M G Farquhar
University of California, San Diego · USNiigata University · JP

Funding

GLOMERULAR CAPILLARIES--NORMAL &PATHOLOGICR01DK017724 · NIDDK · YALE UNIVERSITY · PI FARQUHAR, MARILYN GIST · 1986 to 2008
$3.6M
Glomerular Capillaries-- Normal and PathologicR37DK017724 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FARQUHAR, MARILYN GIST · 2009 to 2015
$2.7M
NIDDK NIH HHS DK-17724NIDDK NIH HHS R01 DK017724NIDDK NIH HHS R37 DK017724
6 · The paper itself

Abstract

Podocalyxin (PC), the major sialoprotein of glomerular epithelial cells (GECs), helps maintain the characteristic architecture of the foot processes and the patency of the filtration slits. PC associates with actin via ezrin, a member of the ERM family of cytoskeletal linker proteins. Here we show that PC is linked to ezrin and the actin cytoskeleton via Na(+)/H(+)-exchanger regulatory factor 2 (NHERF2), a scaffold protein containing two PDZ (PSD-95/Dlg/ZO-1) domains and an ERM-binding region. The cytoplasmic tail of PC contains a C-terminal PDZ-binding motif (DTHL) that binds to the second PDZ domain of NHERF2 in yeast two-hybrid and in vitro pull-down assays. By immunocytochemistry NHERF2 colocalizes with PC and ezrin along the apical domain of the GEC plasma membrane. NHERF2 and ezrin form a multimeric complex with PC, as they coimmunoprecipitate with PC. The PC/NHERF2/ezrin complex interacts with the actin cytoskeleton, and this interaction is disrupted in GECs from puromycin aminonucleoside-, protamine sulfate-, or sialidase-treated rats, which show a dramatic loss of foot processes, comparable to that seen in the nephrotic syndrome. Thus NHERF2 appears to function as a scaffold protein linking PC to ezrin and the actin cytoskeleton. PC/NHERF2/ezrin/actin interactions are disrupted in pathologic conditions associated with changes in GEC foot processes, indicating their importance for maintaining the unique organization of this epithelium.

Indexed as

ActinsAnimalsBinding SitesCell MembraneCells, CulturedCytoskeletal ProteinsCytoskeletonDNA, ComplementaryEpithelial CellsEzrinImmunohistochemistryKidney GlomerulusMaleMolecular Sequence DataNephrotic SyndromePhosphoproteinsActinsCytoskeletal ProteinsDNA, ComplementaryEzrinPhosphoproteinspodocalyxinSialoglycoproteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID11457882
PMCPMC203027
OpenAlexW1981012330

What OpenQuestion holds

Textmetadata
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.