Evidence map›Paper›PMID 18764819›Full record

ArticleTraffic (Copenhagen, Denmark)2008

A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.

Sandra Maday, Eric Anderson, Henry C Chang, James Shorter, Ayano Satoh, Jeff Sfakianos, Heike Fölsch, James M Anderson, Zenta Walther, Ira Mellman

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. An Atlas of Heparan Sulfate Proteoglycans in the Postnatal Rat Lens.Investigative ophthalmology & visual science · 2021
    Article
  4. Article
  5. Review
  6. Article
  7. The Golgin Protein Giantin Regulates Interconnections Between Golgi Stacks.Frontiers in cell and developmental biology · 2019
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. ALP/Enigma PDZ-LIM domain proteins in the heart.Journal of molecular cell biology · 2010
    Review
  20. 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

10 authors at 6 institutions in 1 country.

Sandra MadayDepartment of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA.
Eric Anderson
Henry C Chang
James Shorter
Ayano Satoh
Jeff Sfakianos
Heike Fölsch
James M Anderson
Zenta Walther
Ira Mellman
Yale University · USLudwig Cancer Research · USNorthwestern University · USPurdue University West Lafayette · USUniversity of North Carolina at Chapel Hill · USUniversity of Pennsylvania · US

Funding

ROLE OF YPT5 INTERACTING COMPONENTS IN ENDOCYTOSISP01CA046128 · NCI · YALE UNIVERSITY · PI NOVICK, PETER JAY · 1988 to 2007
$9.5M
MOLECULAR SORTING DURING INTRACELLULAR TRANSPORTR01GM029765 · NIGMS · YALE UNIVERSITY · PI MELLMAN, IRA S · 1985 to 2006
$2.6M
Molecular and Functional Analysis of CASK in EpitheliaK08DK059341 · NIDDK · YALE UNIVERSITY · PI WALTHER, ZENTA · 2001 to 2005
$653k
NCI NIH HHS P01 CA046128NCI NIH HHS P01CA461285NIDDK NIH HHS K08 DK059341NIDDK NIH HHS K08DK059341NIGMS NIH HHS R01 GM029765NIGMS NIH HHS R01GM29765
6 · The paper itself

Abstract

The cell surface proteoglycan, syndecan-1, is essential for normal epithelial morphology and function. Syndecan-1 is selectively localized to the basolateral domain of polarized epithelial cells and interacts with cytosolic PDZ (PSD-95, discs large, ZO-1) domain-containing proteins. Here, we show that the polarity of syndecan-1 is determined by its type II PDZ-binding motif. Mutations within the PDZ-binding motif lead to the mislocalization of syndecan-1 to the apical surface. In contrast to previous examples, however, PDZ-binding motif-dependent polarity is not determined by retention at the basolateral surface but rather by polarized sorting prior to syndecan-1's arrival at the plasma membrane. Although none of the four known PDZ-binding partners of syndecan-1 appears to control basolateral localization, our results show that the PDZ-binding motif of syndecan-1 is decoded along the biosynthetic pathway establishing a potential role for PDZ-mediated interactions in polarized sorting.

Indexed as

Amino Acid MotifsPDZ DomainsAnimalsBasement MembraneCell LineDogsEpithelial CellsGene Knockdown TechniquesMutationSyndecan-1Syndecan-1

Identifiers

PMID18764819
PMCPMC2820280
OpenAlexW2075651160

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.