Evidence map›Paper›PMID 21228104›Full record

ReviewAmerican journal of physiology. Renal physiology2011

Protein complexes that control renal epithelial polarity.

Jay Pieczynski, Ben Margolis

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Renal physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Scribble scrambles parathyroid hormone receptor interactions to regulate phosphate and vitamin D homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Drug transport across the blood-testis barrier.American journal of translational research · 2022
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. The Crumbs3 Polarity Protein.Cold Spring Harbor perspectives in biology · 2018
    Review
  20. Regulation of Cell Polarity by Exocyst-Mediated Trafficking.Cold Spring Harbor perspectives in biology · 2018
    Review

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

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

2 authors at 1 institution in 1 country.

Jay PieczynskiDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
Ben Margolis
University of Michigan–Ann Arbor · US

Funding

Crumbs3 in epithelial polarity and ciliogenesisR01DK069605 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARGOLIS, BENJAMIN L · 2005 to 2013
$2.9M
Tight Junction Proteins and Epithelial PolarityR01DK058208 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARGOLIS, BENJAMIN L · 2001 to 2009
$2.2M
Novel Cilia Trafficking MechanismsR01DK084725 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARGOLIS, BENJAMIN L · 2009 to 2010
$702k
NIDDK NIH HHS DK084725NIDDK NIH HHS DK58208NIDDK NIH HHS DK69605NIDDK NIH HHS R01 DK069605
6 · The paper itself

Abstract

Establishment of epithelial apicobasal polarity is crucial for proper kidney development and function. In recent years, there have been important advances in our understanding of the factors that mediate the initiation of apicobasal polarization. Key among these are the polarity complexes that are evolutionarily conserved from simple organisms to humans. Three of these complexes are discussed in this review: the Crumbs complex, the Par complex, and the Scribble complex. The apical Crumbs complex consists of three proteins, Crumbs, PALS1, and PATJ, whereas the apical Par complex consists of Par-3, Par-6, and atypical protein kinase C. The lateral Scribble complex consists of Scribble, discs large, and lethal giant larvae. These complexes modulate kinase and small G protein activity such that the apical and basolateral complexes signal antagonistically, leading to the segregation of the apical and basolateral membranes. The polarity complexes also serve as scaffolds to direct and retain proteins at the apical membrane, the basolateral membrane, or the intervening tight junction. There is plasticity in apicobasal polarity, and this is best seen in the processes of epithelial-to-mesenchymal transition and the converse mesenchymal-to-epithelial transition. These transitions are important in kidney disease as well as kidney development, and modulation of the polarity complexes are critical for these transitions.

Indexed as

Cell MembraneCell PolarityEpithelial CellsEye ProteinsHumansKidneyMembrane ProteinsMultiprotein ComplexesNeoplasm ProteinsNerve Tissue ProteinsTumor Suppressor ProteinsCRB1 protein, humanEye ProteinsJTB protein, humanMembrane ProteinsMultiprotein ComplexesNeoplasm ProteinsNerve Tissue ProteinsSCRIB protein, humanTumor Suppressor Proteins

Identifiers

PMID21228104
PMCPMC3064137
OpenAlexW2123153844

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.