Evidence map›Paper›PMID 23861394›Full record

ArticleThe Journal of biological chemistry2013

Lipid segregation and membrane budding induced by the peripheral membrane binding protein annexin A2.

Patrick Drücker, Milena Pejic, Hans-Joachim Galla, Volker Gerke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 100 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Annexin A2 Contributes to Release of Extracellular Vimentin in Response to Inflammation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Review
  6. Article
  7. Opportunistic pathogeniScience · 2024
    Article
  8. Article
  9. CaProteins · 2023
    Article
  10. Article
  11. Review
  12. CaAdvances in experimental medicine and biology · 2023
    Article
  13. Annexin A7 mediates lysosome repair independently of ESCRT-III.Frontiers in cell and developmental biology · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

Patrick DrückerInstitute of Biochemistry, University of Muenster, Wilhelm-Klemm-Strasse, D-48149 Muenster, Germany.
Milena Pejic
Hans-Joachim Galla
Volker Gerke
University of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of dynamic membrane microdomains is an important phenomenon in many signal transduction and membrane trafficking events. It is driven by intrinsic properties of membrane lipids and integral as well as membrane-associated proteins. Here we analyzed the ability of one peripherally associated membrane protein, annexin A2 (AnxA2), to induce the formation of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-rich domains in giant unilamellar vesicles (GUVs) of complex lipid composition. AnxA2 is a cytosolic protein that can bind PI(4,5)P2 and other acidic phospholipids in a Ca(2+)-dependent manner and that has been implicated in cellular membrane dynamics in endocytosis and exocytosis. We show that AnxA2 binding to GUVs induces lipid phase separation and the recruitment of PI(4,5)P2, cholesterol and glycosphingolipids into larger clusters. This property is observed for the full-length monomeric protein, a mutant derivative comprising the C-terminal protein core domain and for AnxA2 residing in a heterotetrameric complex with its intracellular binding partner S100A10. All AnxA2 derivatives inducing PI(4,5)P2 clustering are also capable of forming interconnections between PI(4,5)P2-rich microdomains of adjacent GUVs. Furthermore, they can induce membrane indentations rich in PI(4,5)P2 and inward budding of these membrane domains into the lumen of GUVs. This inward vesiculation is specific for AnxA2 and not shared with other PI(4,5)P2-binding proteins such as the pleckstrin homology (PH) domain of phospholipase Cδ1. Together our results indicate that annexins such as AnxA2 can efficiently induce membrane deformations after lipid segregation, a mechanism possibly underlying annexin functions in membrane trafficking.

Indexed as

Annexin A2HumansMembrane MicrodomainsMembranes, ArtificialPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaS100 Calcium Binding Protein A10S100 ProteinsAnnexin A2ANXA2 protein, humanMembranes, ArtificialPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPLCD1 protein, humanS100 Calcium Binding Protein A10S100 ProteinsAnnexinCalciumGiant Unilamellar VesiclesLipid RaftMembrane BuddingMembrane CurvatureMembrane StructureMicrodomainPhosphatidylinositol 4,5-BisphosphatePhospholipid Vesicle

Identifiers

PMID23861394
PMCPMC3750172
OpenAlexW2006993557

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.