Evidence map›Paper›PMID 10468577›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

A tubular endosomal fraction from rat liver: biochemical evidence of receptor sorting by default.

M Vergés, R J Havel, K E Mostov

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 45 citations in OpenAlex.

  1. CaAdvances in experimental medicine and biology · 2023
    Article
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  4. Review
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  6. Retromer.Current opinion in cell biology · 2008
    Review
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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

3 authors at 1 institution in 1 country.

M VergésCardiovascular Research Institute and Department of Anatomy, Biochemistry, and Biophysics, University of California, 513 Parnassus Avenue, San Francisco, CA 94143-0452, USA.
R J Havel
K E Mostov
University of California, San Francisco · US

Funding

REGULATION OF TRANSCYTOSIS OF POLYMERIC IMMUNOGLOBULINSR01AI036953 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MOSTOV, KEITH E · 1995 to 2009
$2.5M
TRANSPORT OF IMMUNOGOBULINS ACROSS EPITHELIAL CELLSR01AI025144 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI MOSTOV, KEITH E. · 1987 to 2001
$659k
NIAID NIH HHS R01 AI025144NIAID NIH HHS R01 AI036953NIAID NIH HHS R01AI25144NIAID NIH HHS R01AI36953
6 · The paper itself

Abstract

We previously have isolated an endosomal fraction from rat liver, termed receptor-recycling compartment (RRC), which is highly enriched in recycling receptors and in the transcytotic polymeric Ig receptor (pIgR). We now have analyzed the RRC fraction by immunoisolation and found that no uniquely transcytotic elements were present, because recycling receptors and the pIgR were coisolated on the same elements. In addition, RRC was very rich in proteins previously shown to be associated with recycling endosomes, such as rab 11, cellubrevin, and endobrevin, but relatively poor in early endosome antigen 1. As RRC contains mainly tubules and small vesicles, our results indicate that it is enriched in elements of a tubular endosomal compartment involved in receptor sorting. Biochemical analysis showed that the density of recycling receptors and transcytotic pIgR in RRC membranes was similar to that in early endosome membranes. This observation supports the idea that increasing membrane surface area by endosome tubulation is the main mechanism to ensure efficient receptor sorting and, at the same time, locates RRC in a common step of the endocytotic system before final receptor segregation into distinct recycling and transcytotic pathways.

Indexed as

AnimalsEndocytosisEndosomesEthinyl EstradiolImmunomagnetic SeparationKineticsLigandsLiverMaleRatsRats, Sprague-DawleyReceptors, Cell SurfaceReceptors, FcReceptors, LDLReceptors, TransferrinEthinyl EstradiolIgA receptorLigandsReceptors, Cell SurfaceReceptors, FcReceptors, LDLReceptors, Transferrin

Identifiers

PMID10468577
PMCPMC17857
OpenAlexW1973478930

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.