Evidence map›Paper›PMID 18165318›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Clathrin light chains function in mannose phosphate receptor trafficking via regulation of actin assembly.

Viviane Poupon, Martine Girard, Valerie Legendre-Guillemin, Sebastien Thomas, Lyne Bourbonniere, Jacynthe Philie, Nicholas A Bright, Peter S McPherson

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 89 citations in OpenAlex.

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  10. Clathrin Light Chains: Not to Be Taken so Lightly.Frontiers in cell and developmental biology · 2021
    Review
  11. Clathrin light chain diversity regulates membrane deformation in vitro and synaptic vesicle formation in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Review
  14. Article
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  17. Review
  18. Clathrin light chains' role in selective endocytosis influences antibody isotype switching.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
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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

8 authors at 3 institutions in 2 countries.

Viviane PouponDepartment of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Martine Girard
Valerie Legendre-Guillemin
Sebastien Thomas
Lyne Bourbonniere
Jacynthe Philie
Nicholas A Bright
Peter S McPherson
McGill University · CAMontreal Neurological Institute and Hospital · CAUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin-coated vesicles (CCVs) are major carriers for endocytic cargo and mediate important intracellular trafficking events at the trans-Golgi network (TGN) and endosomes. Whereas clathrin heavy chain provides the structural backbone of the clathrin coat, the role of clathrin light chains (CLCs) is poorly understood. We now demonstrate that CLCs are not required for clathrin-mediated endocytosis but are critical for clathrin-mediated trafficking between the TGN and the endosomal system. Specifically, CLC knockdown (KD) causes the cation-independent mannose-6 phosphate receptor (CI-MPR) to cluster near the TGN leading to a delay in processing of the lysosomal hydrolase cathepsin D. A recently identified binding partner for CLCs is huntingtin-interacting protein 1-related (HIP1R), which is required for productive interactions of CCVs with the actin cytoskeleton. CLC KD causes mislocalization of HIP1R and overassembly of actin, which accumulates in patches around the clustered CI-MPR. A dominant-negative CLC construct that disrupts HIP1R/CLC interactions causes similar alterations in CI-MPR trafficking and actin assembly. Thus, in mammalian cells CLCs function in intracellular membrane trafficking by acting as recruitment proteins for HIP1R, enabling HIP1R to regulate actin assembly on clathrin-coated structures.

Indexed as

ActinsAnimalsBiological TransportCathepsin DCD8 AntigensChlorocebus aethiopsClathrin Light ChainsCOS CellsEndocytosisGolgi ApparatusHeLa CellsHumansLectins, C-TypeMannose-Binding LectinsMannose ReceptorModels, BiologicalActinsCathepsin DCD8 AntigensClathrin Light ChainsHAP1 protein, humanLectins, C-TypeMannose-Binding LectinsMannose ReceptorNerve Tissue ProteinsReceptors, Cell SurfaceRNA, Small Interfering

Identifiers

PMID18165318
PMCPMC2224180
OpenAlexW2008709207

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.