Evidence map›Paper›PMID 2136859›Full record

ArticleThe Journal of cell biology1990

Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry.

T Nakata, K Sobue, N Hirokawa

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 182 citations in OpenAlex.

  1. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  2. Article
  3. Review
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  5. Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. A lipid-protein hybrid model for tight junction.American journal of physiology. Renal physiology · 2008
    Review
  10. Article
  11. Article
  12. Article
  13. S100 protein subcellular localization during epidermal differentiation and psoriasis.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2003
    Article
  14. The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
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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

3 authors at 1 institution in 1 country.

T NakataDepartment of Anatomy and Cell Biology, School of Medicine, University of Tokyo, Japan.
K Sobue
N Hirokawa
Tokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calpactin I complex, a calcium-dependent phospholipid-binding protein, promotes aggregation of chromaffin vesicles at physiological micromolar calcium ion levels. Calpactin I complex was found to be a globular molecule with a diameter of 10.7 +/- 1.7 (SD) nm on mica. When liposomes were aggregated by calpactin, quick-freeze, deep-etching revealed fine thin strands (6.5 +/- 1.9 [SD] nm long) cross-linking opposing membranes in addition to the globules on the surface of liposomes. Similar fine strands were also observed between aggregated chromaffin vesicles when they were mixed with calpactin in the presence of Ca2+ ion. In cultured chromaffin cells, similar cross-linking short strands (6-10 nm) were found between chromaffin vesicles and the plasma membrane after stimulation with acetylcholine. Plasma membranes also revealed numerous globular structures approximately 10 nm in diameter on their cytoplasmic surface. Immunoelectron microscopy on frozen ultrathin sections showed that calpactin I was closely associated with the inner face of the plasma membranes and was especially conspicuous between plasma membranes and adjacent vesicles in chromaffin cells. These in vivo and in vitro data strongly suggest that calpactin I complex changes its conformation to cross-link vesicles and the plasma membrane after stimulation of cultured chromaffin cells.

Indexed as

ExocytosisAdrenal MedullaAnimalsAnnexinsBlotting, WesternCalcium-Binding ProteinsCattleCell MembraneCells, CulturedCytoskeletonFluorescent Antibody TechniqueFreeze EtchingImmunohistochemistryMembrane ProteinsMicroscopy, ElectronProtein ConformationAnnexinsCalcium-Binding ProteinsMembrane Proteins

Identifiers

PMID2136859
PMCPMC2115994
OpenAlexW2102686118

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.