Evidence map›Paper›PMID 11042114›Full record

ArticleThe Biochemical journal2000

Transmembrane and cytoplasmic domains of syndecan mediate a multi-step endocytic pathway involving detergent-insoluble membrane rafts.

I V Fuki, M E Meyer, K J Williams

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

64 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
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  7. The heparan sulfate proteoglycan grip on hyperlipidemia and atherosclerosis.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
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  17. Review
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  19. Article
  20. Syndecan-4 signaling at a glance.Journal of cell science · 2013
    Review

4 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

3 authors at 1 institution in 1 country.

I V FukiDorrance H. Hamilton Research Laboratories, Division of Endocrinology, Diabetes and Metabolic Diseases, Department of Medicine, Jefferson Medical College, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107-679, USA.
M E Meyer
K J Williams
Thomas Jefferson University · US

Funding

ENDOTHELIAL MATRIX IN ATHEROGENESISR01HL058884 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI WILLIAMS, KEVIN JON · 1998 to 2001
$638k
LIPOPROTEIN LIPASE AND ATHEROGENESISR01HL038956 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI WILLIAMS, KEVIN JON · 1994 to 1998
–
METABOLISM OF A SYNTHETIC ANTI-ATHEROGENIC LIPOPROTEINR29HL038956 · NHLBI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI WILLIAMS, KEVIN JON · 1987 to 1991
–
NHLBI NIH HHS HL38956NHLBI NIH HHS HL58884
6 · The paper itself

Abstract

Syndecan heparan sulphate proteoglycans directly mediate a novel endocytic pathway. Using Chinese hamster ovary cells expressing the human syndecan 1 core protein or a chimaeric receptor, FcR-Synd, consisting of the ectodomain of the IgG Fc receptor Ia linked to the transmembrane and cytoplasmic domains of syndecan 1, we previously reported that efficient internalization is triggered by ligand clustering, requires intact actin microfilaments and tyrosine kinases, proceeds with a t(1/2) of approx. 1 h and is distinct from coated-pit pathways. We have now examined the involvement of cholesterol-rich, detergent-insoluble membrane rafts. On clustering, (125)I-labelled IgG bound to FcR-Synd rapidly became insoluble in cold Triton X-100, well before endocytosis. Insolubility of clustered FcR-Synd ligand did not require the syndecan ectodomain, linkage of the cytoplasmic tail to the cytoskeleton, or energy-dependent cellular metabolism. Pretreatment of cells with cyclodextrin to deplete cholesterol from rafts abolished insolubility of the clustered ligand and inhibited endocytosis in a dose-responsive fashion. Similar results were obtained with (125)I-labelled lipoprotein lipase bound to authentic cell-surface syndecan. In contrast, the 39 kDa receptor-associated protein (RAP), a coated-pit ligand, was more than 80% soluble in cold Triton even after internalization; cellular cholesterol depletion failed to substantially affect the internalization of (125)I-RAP. Overall, our results indicate a multi-step endocytic process consisting of ligand binding, clustering, energy-independent lateral movement into detergent-insoluble membrane rafts and finally recruitment of actin and tyrosine kinases to bring the ligands into the cell.

Indexed as

EndocytosisAnimalsCell MembraneCHO CellsCholesterolCricetinaeCytoplasmDetergentsMembrane GlycoproteinsMembrane LipidsProteoglycansSolubilitySyndecan-1SyndecansCholesterolDetergentsMembrane GlycoproteinsMembrane LipidsProteoglycansSDC1 protein, humanSyndecan-1Syndecans

Identifiers

PMID11042114
PMCPMC1221399
OpenAlexW1991172636

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.