Evidence map›Paper›PMID 16087710›Full record

ArticleThe Journal of cell biology2005

Transcytosis of NgCAM in epithelial cells reflects differential signal recognition on the endocytic and secretory pathways.

Eric Anderson, Sandra Maday, Jeff Sfakianos, Michael Hull, Bettina Winckler, David Sheff, Heike Fölsch, Ira Mellman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Novel function for AP-1B during cell migration.Molecular biology of the cell · 2020
    Article
  4. Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020
    Review
  5. Article
  6. Article
  7. Significance of transcytosis in Alzheimer's disease: BACE1 takes the scenic route to axons.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Article
  8. Adaptor proteins involved in polarized sorting.The Journal of cell biology · 2014
    Review
  9. Article
  10. Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2012
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Trafficking guidance receptors.Cold Spring Harbor perspectives in biology · 2010
    Review
  17. Article
  18. Axonal targeting of Trk receptors via transcytosis regulates sensitivity to neurotrophin responses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  19. Article
  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

8 authors at 2 institutions in 1 country.

Eric AndersonDepartment of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA.
Sandra Maday
Jeff Sfakianos
Michael Hull
Bettina Winckler
David Sheff
Heike Fölsch
Ira Mellman
Yale University · USLudwig Cancer Research · US

Funding

MOLECULAR SORTING DURING INTRACELLULAR TRANSPORTR01GM029765 · NIGMS · YALE UNIVERSITY · PI MELLMAN, IRA S · 1985 to 2006
$2.6M
NIGMS NIH HHS GM29765NIGMS NIH HHS R01 GM029765
6 · The paper itself

Abstract

NgCAM is a cell adhesion molecule that is largely axonal in neurons and apical in epithelia. In Madin-Darby canine kidney cells, NgCAM is targeted to the apical surface by transcytosis, being first inserted into the basolateral domain from which it is internalized and transported to the apical domain. Initial basolateral transport is mediated by a sequence motif (Y(33)RSL) decoded by the AP-1B clathrin adaptor complex. This motif is a substrate in vitro for tyrosine phosphorylation by p60src, a modification that disrupts NgCAM's ability to interact with clathrin adaptors. Based on the behavior of various NgCAM mutants, it appears that after arrival at the basolateral surface, the AP-1B interaction site is silenced by phosphorylation of Tyr(33). This slows endocytosis and inhibits basolateral recycling from endosomes, resulting in NgCAM transcytosis due to a cryptic apical targeting signal in its extracellular domain. Thus, transcytosis of NgCAM and perhaps other membrane proteins may reflect the spatial regulation of recognition by adaptors such as AP-1B.

Indexed as

EndocytosisSignal TransductionAdaptor Protein Complex 1Amino Acid SequenceAnimalsCell Adhesion MoleculesCell PolarityCytoplasmDogsEpithelial CellsMolecular Sequence DataPhosphotyrosineProtein BindingProtein Structure, TertiaryProtein TransportAdaptor Protein Complex 1Cell Adhesion MoleculesPhosphotyrosine

Identifiers

PMID16087710
PMCPMC2171499
OpenAlexW2095280415

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.