Evidence map›Paper›PMID 24407285›Full record

ArticleThe Journal of biological chemistry2014

Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors.

Wiebke Stahlschmidt, Mark J Robertson, Phillip J Robinson, Adam McCluskey, Volker Haucke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The Noonan Syndrome GeneCirculation research · 2020
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Building endocytic pits without clathrin.Nature reviews. Molecular cell biology · 2015
    Review
  12. Article
  13. Article
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 4 institutions in 2 countries.

Wiebke StahlschmidtFrom the Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin-Buch, Germany.
Mark J Robertson
Phillip J Robinson
Adam McCluskey
Volker Haucke
University of Newcastle Australia · AULeibniz-Forschungsinstitut für Molekulare Pharmakologie · DELeibniz Institute for Neurobiology · DEUniversity of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin plays important roles in intracellular membrane traffic including endocytosis of plasma membrane proteins and receptors and protein sorting between the trans-Golgi network (TGN) and endosomes. Whether clathrin serves additional roles in receptor recycling, degradative sorting, or constitutive secretion has remained somewhat controversial. Here we have used acute pharmacological perturbation of clathrin terminal domain (TD) function to dissect the role of clathrin in intracellular membrane traffic. We report that internalization of major histocompatibility complex I (MHCI) is inhibited in cells depleted of clathrin or its major clathrin adaptor complex 2 (AP-2), a phenotype mimicked by application of Pitstop® inhibitors of clathrin TD function. Hence, MHCI endocytosis occurs via a clathrin/AP-2-dependent pathway. Acute perturbation of clathrin also impairs the dynamics of intracellular clathrin/adaptor complex 1 (AP-1)- or GGA (Golgi-localized, γ-ear-containing, Arf-binding protein)-coated structures at the TGN/endosomal interface, resulting in the peripheral dispersion of mannose 6-phosphate receptors. By contrast, secretory traffic of vesicular stomatitis virus G protein, recycling of internalized transferrin from endosomes, or degradation of EGF receptor proceeds unperturbed in cells with impaired clathrin TD function. These data indicate that clathrin is required for the function of AP-1- and GGA-coated carriers at the TGN but may be dispensable for outward traffic en route to the plasma membrane.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Proteins, Vesicular TransportAnimalsCattleClathrinCoated Pits, Cell-MembraneCoat Protein Complex IEndocytosisEndosomesErbB ReceptorsGreen Fluorescent ProteinsHeLa CellsHistocompatibility Antigens Class IHumansMembrane GlycoproteinsAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Proteins, Vesicular TransportClathrinCoat Protein Complex IErbB ReceptorsGGA adaptor proteinsG protein, vesicular stomatitis virusGreen Fluorescent ProteinsHistocompatibility Antigens Class IMembrane Glycoproteinspitstop 2Receptor, IGF Type 2SulfonamidesThiazolidinesTransferrinViral Envelope ProteinsCell BiologyEndosomesLysosomesMembrane TraffickingMolecular Cell BiologyProtein Sorting

Identifiers

PMID24407285
PMCPMC3931052
OpenAlexW2017123140

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.