Evidence map›Paper›PMID 29930080›Full record

ArticleJournal of cell science2018

Transbilayer phospholipid movement facilitates the translocation of annexin across membranes.

Sarah E Stewart, Avraham Ashkenazi, Athena Williamson, David C Rubinsztein, Kevin Moreau

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. CaAdvances in experimental medicine and biology · 2023
    Article
  8. Review
  9. Unconventional Pathways of Protein Secretion: MammalsFrontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Through the back door: Unconventional protein secretion.Cell surface (Amsterdam, Netherlands) · 2020
    Review
  14. Article
  15. Unconventional secretion of annexins and galectins.Seminars in cell & developmental biology · 2018
    Review
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

5 authors at 1 institution in 1 country.

Sarah E StewartUniversity of Cambridge, Metabolic Research Laboratories, Wellcome Trust-Medical Research Council Institute of Metabolic Science, Cambridge, CB2 0QQ, UK.
Avraham AshkenaziUniversity of Cambridge, Department of Medical Genetics, Cambridge Institute for Medical Research, Wellcome/MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge CB2 0XY, UK.
Athena WilliamsonUniversity of Cambridge, Metabolic Research Laboratories, Wellcome Trust-Medical Research Council Institute of Metabolic Science, Cambridge, CB2 0QQ, UK.
David C RubinszteinUniversity of Cambridge, Department of Medical Genetics, Cambridge Institute for Medical Research, Wellcome/MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge CB2 0XY, UK km510@cam.ac.uk dcr1000@cam.ac.uk.
Kevin MoreauUniversity of Cambridge, Metabolic Research Laboratories, Wellcome Trust-Medical Research Council Institute of Metabolic Science, Cambridge, CB2 0QQ, UK km510@cam.ac.uk dcr1000@cam.ac.uk.ORCID 0000-0002-3688-3998
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P010911/1Medical Research Council MC_UU_00014/5Medical Research Council MC_UU_12012/1Medical Research Council MC_UU_12012/5Medical Research Council MR/N501827/1Medical Research Council UKDRI-2002
6 · The paper itself

Abstract

Annexins are cytosolic phospholipid-binding proteins that can be found on the outer leaflet of the plasma membrane. The extracellular functions of annexin include modulating fibrinolysis activity and cell migration. Despite having well-described extracellular functions, the mechanism of annexin transport from the cytoplasmic inner leaflet to the extracellular outer leaflet of the plasma membrane remains unclear. Here, we show that the transbilayer movement of phospholipids facilitates the transport of annexins A2 and A5 across membranes in cells and in liposomes. We identified TMEM16F (also known as anoctamin-6, ANO6) as a lipid scramblase required for transport of these annexins to the outer leaflet of the plasma membrane. This work reveals a mechanism for annexin translocation across membranes which depends on plasma membrane phospholipid remodelling.

Indexed as

Annexin A2Annexin A5AnoctaminsCell MembraneHeLa CellsHumansLipid BilayersLiposomesPhospholipidsPhospholipid Transfer ProteinsProtein TransportAnnexin A2Annexin A5ANO6 protein, humanAnoctaminsLipid BilayersLiposomesPhospholipidsPhospholipid Transfer ProteinsAnnexinLipid flippingProtein translocationTMEM16F

Identifiers

PMID29930080
PMCPMC6080606
OpenAlexW2808731252

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.