Evidence map›Paper›PMID 21737841›Full record

ArticleThe Journal of biological chemistry2011

Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2.

Mallika Valapala, Jamboor K Vishwanatha

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

119 citing papers in PubMed, 199 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Frontiers in immunology · 2026
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

59 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

2 authors at 2 institutions in 1 country.

Mallika ValapalaDepartments of Biomedical Sciences, Fort Worth, Texas 76107.
Jamboor K VishwanathaDepartments of Biomedical Sciences, Fort Worth, Texas 76107; Molecular Biology and Immunology, Fort Worth, Texas 76107; Institute for Cancer Research, University of North Texas Health Science Center, Fort Worth, Texas 76107. Electronic address: Jamboor.vishwanatha@unthsc.edu.
Fort Worth Library · USUniversity of North Texas Health Science Center · US

Funding

Visceral Fat & Lipid & Inflammatory Risk factors: Role of EthnicityP20MD001633 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI GONZALEZ, ADELA · 2005 to 2009
$7.1M
Triple Negative Breast Cancer: Novel Biomarkers and Therapeutic StrategiesP20MD006882 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI GHORPADE, ANUJA · 2012 to 2016
$5.8M
NIMHD NIH HHS MD001633NIMHD NIH HHS P20 MD001633NIMHD NIH HHS P20 MD006882
6 · The paper itself

Abstract

Annexin A2 (AnxA2), a Ca(2+)-dependent phospholipid-binding protein, is known to associate with the plasma membrane and the endosomal system. Within the plasma membrane, AnxA2 associates in a Ca(2+) dependent manner with cholesterol-rich lipid raft microdomains. Here, we show that the association of AnxA2 with the lipid rafts is influenced not only by intracellular levels of Ca(2+) but also by N-terminal phosphorylation at tyrosine 23. Binding of AnxA2 to the lipid rafts is followed by the transport along the endocytic pathway to be associated with the intralumenal vesicles of the multivesicular endosomes. AnxA2-containing multivesicular endosomes fuse directly with the plasma membrane resulting in the release of the intralumenal vesicles into the extracellular environment, which facilitates the exogenous transfer of AnxA2 from one cell to another. Treatment with Ca(2+) ionophore triggers the association of AnxA2 with the specialized microdomains in the exosomal membrane that possess raft-like characteristics. Phosphorylation at Tyr-23 is also important for the localization of AnxA2 to the exosomal membranes. These results suggest that AnxA2 is trafficked from the plasma membrane rafts and is selectively incorporated into the lumenal membranes of the endosomes to escape the endosomal degradation pathway. The Ca(2+)-dependent exosomal transport constitutes a novel pathway of extracellular transport of AnxA2.

Indexed as

EndocytosisAnimalsAnnexin A2Biological TransportBiotinylationCalciumCalcium-Binding ProteinsCell Line, TumorCell MembraneCentrifugation, Density GradientExosomesExtracellular MatrixIonophoresMembrane MicrodomainsMiceMicroscopy, ConfocalAnnexin A2CalciumCalcium-Binding ProteinsIonophoresSucroseTyrosine

Identifiers

PMID21737841
PMCPMC3162451
OpenAlexW2083757415

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.