Evidence map›Paper›PMID 9188103›Full record

ArticleMolecular biology of the cell1997

Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol.

T Harder, R Kellner, R G Parton, J Gruenberg

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.0field-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

64 citing papers in PubMed, 210 citations in OpenAlex.

  1. Review
  2. Holistic Investigation of Graphene Quantum Dot Endocytosis.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Article
  4. Review
  5. Accumulation of annexin A2 and S100A10 prevents apoptosis of apically delaminated, transformed epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. CaAdvances in experimental medicine and biology · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Annexins-Coordinators of Cholesterol Homeostasis in Endocytic Pathways.International journal of molecular sciences · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013
    Article
  20. Article

4 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

4 authors at 1 institution in 1 country.

T HarderInstitut für Physiologische Chemie und Pathobiochemie, University of Mainz, Germany.
R Kellner
R G Parton
J Gruenberg
Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Annexin II is an abundant protein which is present in the cytosol and on the cytoplasmic face of plasma membrane and early endosomes. It is generally believed that this association occurs via Ca(2+)-dependent binding to lipids, a mechanism typical for the annexin protein family. Although previous studies have shown that annexin II is involved in early endosome dynamics and organization, the precise biological role of the protein is unknown. In this study, we found that approximately 50% of the total cellular annexin was associated with membranes in a Ca(2+)-independent manner. This binding was extremely tight, since it resisted high salt and, to some extent, high pH treatments. We found, however, that membrane-associated annexin II could be quantitatively released by low concentrations of the cholesterol-sequestering agents filipin and digitonin. Both treatments released an identical and limited set of proteins but had no effects on other membrane-associated proteins. Among the released proteins, we identified, in addition to annexin II itself, the cortical cytoskeletal proteins alpha-actinin, ezrin and moesin, and membrane-associated actin. Our biochemical and immunological observations indicate that these proteins are part of a complex containing annexin II and that stability of the complex is sensitive to cholesterol sequestering agents. Since annexin II is tightly membrane-associated in a cholesterol-dependent manner, and since it seems to interact physically with elements of the cortical actin cytoskeleton, we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton.

Indexed as

AnimalsAnnexin A2AvidinCalciumCell LineCell MembraneCholesterolCricetinaeCytoskeletal ProteinsDogsHorseradish PeroxidaseKidneyMembrane LipidsMembrane ProteinsSubcellular FractionsAnnexin A2Avidinavidin-horseradish peroxidase complexCalciumCholesterolCytoskeletal ProteinsHorseradish PeroxidaseMembrane LipidsMembrane Proteins

Identifiers

PMID9188103
PMCPMC276102
OpenAlexW2115666450

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.