Evidence map›Paper›PMID 8601581›Full record

ArticleThe Journal of cell biology1996

Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes.

C E Futter, A Pearse, L J Hewlett, C R Hopkins

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

203 citing papers in PubMed, 532 citations in OpenAlex.

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  13. Bioengineering extracellular vesicle cargo for optimal therapeutic efficiency.Molecular therapy. Methods & clinical development · 2024
    Review
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  19. Review
  20. Review

143 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

C E FutterMedical Research Council Laboratory for Molecular Cell Biology, University College, London, United Kingdom.
A Pearse
L J Hewlett
C R Hopkins
MRC Laboratory for Molecular Cell Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have followed the transfer of EGF-EGF receptor (EGFR) complexes from endosomal vacuoles that contain transferrin receptors (TfR) to lysosome vacuoles identified by their content of HRP loaded as a 15-min pulse 4 h previously. We show that the HRP-loaded lysosomes are lysosomal-associated membrane protein-1 (LAMP-1) positive, mannose-6-phosphate receptor (M6PR) negative. and contain active acid hydrolase. EGF-EGFR complexes are delivered to these lysosomes intact and are then rapidly degraded. Preactivating the HRP contained within the preloaded lysosomes inhibits the delivery of EGFR and degradation of EGF, and results in the accumulation of EGFR-containing multivesicular bodies (MVB). With time these accumulating MVB undergo a series of maturation changes that include the loss of TfR, the continued recruitment of EGFR, and the accumulation of internal vesicles, but they remain LAMP-1 and M6PR negative. The mature MVB are often seen to make direct contact with lysosomes containing preactivated HRP, but their perimeter membranes remain intact. Together our observations suggest that the transfer of EGF-EGFR complexes from the TfR-containing endosome compartment to the lysosomes that degrade them employs a single vacuolar intermediate, the maturing MVB, and can be achieved by a single heterotypic fusion step.

Indexed as

Antigens, CDBiomarkersCell LineEndocytosisEndosomesEpidermal Growth FactorErbB ReceptorsHorseradish PeroxidaseHydrolysisLysosomal Membrane ProteinsLysosomesMembrane FusionMembrane GlycoproteinsMicroscopy, ElectronReceptor, IGF Type 2Receptors, TransferrinAntigens, CDBiomarkersEpidermal Growth FactorErbB ReceptorsHorseradish PeroxidaseLysosomal Membrane ProteinsMembrane GlycoproteinsReceptor, IGF Type 2Receptors, TransferrinRecombinant Proteins

Identifiers

PMID8601581
PMCPMC2120766
OpenAlexW2082543204

What OpenQuestion holds

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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.