Evidence map›Paper›PMID 14699065›Full record

ArticleMolecular biology of the cell2004

Specific N-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol-anchored forms of endolyn in Madin-Darby canine kidney cells.

Beth A Potter, Gudrun Ihrke, Jennifer R Bruns, Kelly M Weixel, Ora A Weisz

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014
    Review
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  13. Review
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  15. Role of N-glycosylation in trafficking of apical membrane proteins in epithelia.American journal of physiology. Renal physiology · 2009
    Review
  16. Article
  17. 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

5 authors at 2 institutions in 3 countries.

Beth A PotterLaboratory of Epithelial Cell Biology, Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Gudrun Ihrke
Jennifer R Bruns
Kelly M Weixel
Ora A Weisz
University of Pittsburgh · USUniversity of Cambridge · GB

Funding

Regulation of Apical Traffic in Renal Epithelial CellsR01DK054407 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WEISZ, ORA A · 1998 to 2011
$3.3M
Renal and Epithelial Biology Training ProgramT32DK061296 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2002 to 2022
$3.1M
NIDDK NIH HHS DK-54407NIDDK NIH HHS DK61296NIDDK NIH HHS R01 DK054407NIDDK NIH HHS T32 DK061296Wellcome Trust
6 · The paper itself

Abstract

The sialomucin endolyn is a transmembrane protein with a unique trafficking pattern in polarized Madin-Darby canine kidney cells. Despite the presence of a cytoplasmic tyrosine motif that, in isolation, is sufficient to mediate basolateral sorting of a reporter protein, endolyn predominantly traverses the apical surface en route to lysosomes. Apical delivery of endolyn is disrupted in tunicamycin-treated cells, implicating a role for N-glycosylation in apical sorting. Site-directed mutagenesis of endolyn's eight N-glycosylation sites was used to identify two N-glycans that seem to be the major determinants for efficient apical sorting of the protein. In addition, apical delivery of endolyn was disrupted when terminal processing of N-glycans was blocked using glycosidase inhibitors. Missorting of endolyn occurred independently of the presence or absence of the basolateral sorting signal, because apical delivery was also inhibited by tunicamycin when the cytoplasmic tyrosine motif was mutated. However, we found that apical secretion of a soluble mutant of endolyn was N-glycan independent, as was delivery of glycosylphosphatidylinositol-anchored endolyn. Thus, specific N-glycans are only essential for the apical sorting of transmembrane endolyn, suggesting fundamental differences in the mechanisms by which soluble, glycosylphosphatidylinositol-anchored, and transmembrane proteins are sorted.

Indexed as

AnimalsCD146 AntigenCell MembraneCell PolarityCells, CulturedCytoplasmDogsEndolynGlycosylationGlycosylphosphatidylinositolsMembrane GlycoproteinsMembrane ProteinsPolysaccharidesProtein Sorting SignalsProtein TransportCD146 AntigenEndolynGlycosylphosphatidylinositolsMembrane GlycoproteinsMembrane ProteinsPolysaccharidesProtein Sorting Signals

Identifiers

PMID14699065
PMCPMC363156
OpenAlexW2160764634

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.