Evidence map›Paper›PMID 9188102›Full record

ArticleMolecular biology of the cell1997

Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes.

R P Czekay, R A Orlando, L Woodward, M Lundstrom, M G Farquhar

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cryo-EM structures elucidate the multiligand receptor nature of megalin.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Renal Handling of Albumin-From Early Findings to Current Concepts.International journal of molecular sciences · 2021
    Review
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  11. 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

5 authors at 1 institution in 1 country.

R P CzekayDivision of Cellular and Molecular Medicine, University of California San Diego, La Jolla 92093, USA.
R A Orlando
L Woodward
M Lundstrom
M G Farquhar
University of California San Diego · US

Funding

GLOMERULAR CAPILLARIES--NORMAL &PATHOLOGICR01DK017724 · NIDDK · YALE UNIVERSITY · PI FARQUHAR, MARILYN GIST · 1986 to 2008
$3.6M
NIDDK NIH HHS DK-17724
6 · The paper itself

Abstract

Megalin (gp330) is a member of the low-density lipoprotein receptor gene family. Like other members of the family, it is an endocytic receptor that binds a number of specific ligands. Megalin also binds the receptor-associated protein (RAP) that serves as an exocytic traffic chaperone and inhibits ligand binding to the receptor. To investigate the fate of megalin/RAP complexes, we bound RAP glutathione-S-transferase fusion protein (RAP-GST) to megalin at the surface of L2 yolk sac carcinoma cells and followed the trafficking of the complexes by immunofluorescence and immunogold labeling and by their distribution on Percoll gradients. We show that megalin/RAP-GST complexes, which are internalized via clathrin-coated pits, are delivered to early endosomes where they accumulate during an 18 degrees C temperature block and colocalize with transferrin and transferrin receptor. Upon release from the temperature block, the complexes travel to late endosomes where they colocalize with rab7 and can be coprecipitated with anti-RAP-GST antibodies. Dissociation of the complex occurs in late endosomes and is most likely triggered by the low pH (approximately 5.5) of this compartment. RAP is then rapidly delivered to lysosomes and degraded whereas megalin is recycled to the cell surface. When the ligand, lipoprotein lipase, was bound to megalin, the receptor was found to recycle through early endosomes. We conclude that in contrast to receptor/ligand complexes, megalin/RAP complexes traffic through late endosomes, which is a novelty for members of the low-density lipoprotein receptor gene family.

Indexed as

EndocytosisAnimalsAutoantigensCarrier ProteinsCell CompartmentationEndosomesGlycoproteinsHeymann Nephritis Antigenic ComplexImmunoglobulin Fab FragmentsKidney GlomerulusLDL-Receptor Related Protein-Associated ProteinLysosomesMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesProtein BindingAutoantigensCarrier ProteinsGlycoproteinsHeymann Nephritis Antigenic ComplexImmunoglobulin Fab FragmentsLDL-Receptor Related Protein-Associated ProteinMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesReceptors, LDL

Identifiers

PMID9188102
PMCPMC276101
OpenAlexW1971740096

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.