Evidence map›Paper›PMID 16720734›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2006

Post-translational modification plays an essential role in the translocation of annexin A1 from the cytoplasm to the cell surface.

E Solito, H C Christian, M Festa, A Mulla, T Tierney, R J Flower, J C Buckingham

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

60 citing papers in PubMed, 131 citations in OpenAlex.

  1. A Novel Dysferlin-Binding Kinase CK2α Promotes Plasma Membrane Repair in Dysferlinopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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  19. Annexins in Translational Research: Hidden Treasures to Be Found.International journal of molecular sciences · 2018
    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

7 authors at 5 institutions in 1 country.

E SolitoDepartment of Cellular and Molecular Neuroscience, Division of Neuroscience and Mental Health, Imperial College London, Hammersmith Campus, Du Cane Rd., London W12 0NN, UK.
H C Christian
M Festa
A Mulla
T Tierney
R J Flower
J C Buckingham
Mental Health Research UK · GBImperial College London · GBWilliam Harvey Research Institute · GBCentre for Human Genetics · GBUniversity of Oxford · GB

Funding

Wellcome Trust 040269Wellcome Trust N:069234/B/02/Z
6 · The paper itself

Abstract

Annexin A1 (ANXA1) has an important role in cell-cell communication in the host defense and neuroendocrine systems. In both systems, its actions are exerted extracellularly via membrane-bound receptors on adjacent sites after translocation of the protein from the cytoplasm to the cell surface of adjacent cells. This study used molecular, microscopic, and pharmacological approaches to explore the mechanisms underlying the cellular exportation of ANXA1 in TtT/GF (pituitary folliculo-stellate) cells. LPS caused serine-phosphorylation of ANXA1 (ANXA1-S27-PO4) and translocation of the phosphorylated protein to the cell membrane. The fundamental requirement of phosphorylation for membrane translocation was confirmed by immunofluorescence microscopy on cells transfected with wild-type or mutated (S27/A) ANXA1 constructs tagged with enhanced green fluorescence protein. The trafficking of ANXA1-S27-PO4 to the cell surface was dependent on PI3-kinase and MAP-kinase. It also required HMG-coenzyme A and myristoylation. The effects of HMG-coenzyme A blockade were overcome by mevalonic acid (the product of HMG-coenzyme A) and farnesyl-pyrophosphate but not by geranyl-geranylpyrophosphate or cholesterol. Together, these results suggest that serine-27 phosphorylation is essential for the translocation of ANXA1 across the cell membrane and also identify a role for isoprenyl lipids. Such lipids could target consensus sequences in ANXA1. Alternatively, they may target other proteins in the signal transduction cascade (e.g., transporters).

Indexed as

Protein Processing, Post-TranslationalAnimalsAnnexin A1Cell CommunicationCell Line, TumorCell MembraneCytoplasmEnzyme InhibitorsGenes, ReporterLipopolysaccharidesMevalonic AcidMiceMutagenesis, Site-DirectedPhosphorylationPituitary NeoplasmsProtein TransportAnnexin A1Enzyme InhibitorsLipopolysaccharidesMevalonic Acid

Identifiers

PMID16720734
PMCPMC2049060
OpenAlexW1972811309

What OpenQuestion holds

Textmetadata
LicenceTDM
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.