Evidence map›Paper›PMID 21645192›Full record

ArticleTraffic (Copenhagen, Denmark)2011

Biochemical characterization of APPL endosomes: the role of annexin A2 in APPL membrane recruitment.

Anna Urbanska, Lukasz Sadowski, Yannis Kalaidzidis, Marta Miaczynska

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Revising Endosomal Trafficking under Insulin Receptor Activation.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013
    Article
  16. Article
  17. 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

4 authors at 2 institutions in 2 countries.

Anna UrbanskaInternational Institute of Molecular and Cell Biology, Laboratory of Cell Biology, International Institute of Molecular and Cell Biology, 4 Ks. Trojdena Street, 02-109 Warsaw, Poland.
Lukasz Sadowski
Yannis Kalaidzidis
Marta Miaczynska
International Institute of Molecular and Cell Biology · PLMax Planck Society · DE

Funding

Howard Hughes Medical InstituteWellcome Trust 076469/Z/05/Z
6 · The paper itself

Abstract

APPL endosomes are a recently identified subpopulation of early endosomes characterized by the presence of two homologous Rab5 effector proteins APPL1 and APPL2. They exhibit only limited colocalization with EEA1, another Rab5 effector and a marker of the canonical early endosomes. Although APPL endosomes appear to play important roles in cargo trafficking and signal transduction, their protein composition and biochemical properties remain largely unknown. Here we employed membrane fractionation methods to characterize APPL endosomes biochemically. We demonstrate that they represent heterogeneous membrane structures which can be discriminated from the canonical EEA1-positive early endosomes by their partly different physical properties and a distinct migration pattern in the continuous density gradients. In search for other potential markers of APPL endosomes we identified Annexin A2 as an interacting partner of both APPL1 and APPL2. Annexin A2 is a Ca(2+) and phosphatidylinositol 4,5-bisphosphate binding protein, previously implicated in several endocytic steps. We show that Annexin A2 co-fractionates and colocalizes with APPL endosomes. Moreover, silencing of its expression causes solubilization of APPL2 from endosomes. Although Annexin A2 is not an exclusive marker of APPL endosomes, our data suggest that it has an important function in membrane recruitment of APPL proteins, acting in parallel to Rab5.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAnnexin A2CalciumCell FractionationCell MembraneEndosomesHEK293 CellsHeLa CellsHumansPhosphatidylinositolsrab5 GTP-Binding ProteinsRecombinant Fusion ProteinsRNA InterferenceSubcellular FractionsAdaptor Proteins, Signal TransducingAnnexin A2APPL1 protein, humanAPPL2 protein, humanCalciumPhosphatidylinositolsrab5 GTP-Binding ProteinsRecombinant Fusion Proteins

Identifiers

PMID21645192
PMCPMC3380557
OpenAlexW2129890352

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.