Evidence map›Paper›PMID 8245122›Full record

ArticleThe Journal of cell biology1993

The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex.

T Harder, V Gerke

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 159 citations in OpenAlex.

  1. Review
  2. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  3. Review
  4. Review
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  7. The Biology of Annexin A2: From Vascular Fibrinolysis to Innate Immunity.Transactions of the American Clinical and Climatological Association · 2015
    Review
  8. Article
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  17. Review
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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

2 authors at 1 institution in 1 country.

T HarderMax Planck Institute for Biophysical Chemistry, Department of Biochemistry, Göttingen, FRG.
V Gerke
Max Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tyrosine kinase substrate annexin II is a member of a multigene family of Ca2+ and lipid-binding proteins which have been implicated in a number of membrane-related events. We have analyzed the subcellular distribution of annexin II in relation to other cellular components in normal and specifically manipulated MDCK cells. In a polarized monolayer of MDCK cells annexin II and its cellular ligand p11 are restricted almost exclusively to the cortical regions of the cells which also contain peripheral early endosomes. Treatment of the polarized cells with low Ca2+ medium leads to a disintegration of the cortical cytoskeleton and a translocation of both, the annexin II2p11(2) complex and early endosomes, to the cytoplasm. A similar translocation which is however specific for the annexin II2p11(2) complex and early endosomes and does not affect other elements of the cell cortex is observed in cells expressing a trans-dominant annexin II-p11 mutant. This chimeric mutant protein causes the aggregation of endogenous annexin II and p11 and the simultaneous detachment of early endosomes from the cell periphery resulting in the binding of the early endosomes but no other components of the endocytotic or biosynthetic pathways to the annexin II/p11 aggregates. The specificity of this effect argues for the association of the annexin II2p11(2) complex with early endosomes and suggests that this association contributes to establish the peripheral localization of early endosomal structures.

Indexed as

ActinsAmino Acid SequenceAnimalsAnnexin A2Base SequenceBiological TransportCadherinsCalciumCell PolarityCells, CulturedCytoplasmCytoskeletonDNAEndocytosisIntracellular MembranesMacromolecular SubstancesActinsAnnexin A2CadherinsCalciumDNAMacromolecular SubstancesReceptor, IGF Type 2Receptors, TransferrinRecombinant Fusion Proteins

Identifiers

PMID8245122
PMCPMC2119870
OpenAlexW1969926473

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.