Evidence map›Paper›PMID 19150361›Full record

ArticleJournal of molecular biology2009

Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter.

Adrian E Rice, Michael J Mendez, Craig A Hokanson, Douglas C Rees, Pamela J Björkman

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Iron overload impairs renal function and is associated with vascular calcification in rat aorta.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
    Article
  7. Associated Effect ofMetabolites · 2022
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Inherited iron overload disorders.Translational gastroenterology and hepatology · 2020
    Review
  15. Review
  16. Article
  17. Ferroportin disease mutations influence manganese accumulation and cytotoxicity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  18. Review
  19. Article
  20. 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.

Adrian E RiceGraduate Option in Biochemistry and Molecular Biophysics, California Institute of Technology, Pasadena, CA 91125, USA.
Michael J Mendez
Craig A Hokanson
Douglas C Rees
Pamela J Björkman
California Institute of Technology · US

Funding

HFE/Transferrin Receptor/Transferrin InteractionsR01DK060770 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 2002 to 2006
$1.3M
NIDDK NIH HHS 1R01 DK60770-01NIDDK NIH HHS R01 DK060770
6 · The paper itself

Abstract

Ferroportin is a multipass membrane protein that serves as an iron exporter in many vertebrate cell types. Ferroportin-mediated iron export is controlled by the hormone hepcidin, which binds ferroportin, causing its internalization and degradation. Mutations in ferroportin cause a form of the iron overload hereditary disease hemochromatosis. Relatively little is known about ferroportin's properties or the mechanism by which mutations cause disease. In this study, we expressed and purified human ferroportin to characterize its biochemical/biophysical properties in solution and conducted cell biological studies in mammalian cells. We found that purified detergent-solubilized ferroportin is a well-folded monomer that binds hepcidin. In cell membranes, the N- and C-termini were both cytosolic, implying an even number of transmembrane regions, and ferroportin was mainly localized to the plasma membrane. Hepcidin addition resulted in a redistribution of ferroportin to intracellular compartments that labeled with early endosomal and lysosomal, but not Golgi, markers and that trafficked along microtubules. An analysis of 16 disease-related ferroportin mutants revealed that all were expressed and trafficked to the plasma membrane but that some were resistant to hepcidin-induced internalization. The characterizations reported here form a basis upon which models for ferroportin's role in regulating iron homeostasis in health and disease can be interpreted.

Indexed as

AnimalsAntimicrobial Cationic PeptidesCation Transport ProteinsCell LineCell MembraneEndosomesFerroportinHepcidinsHumansLysosomesModels, BiologicalModels, MolecularMolecular WeightMutant ProteinsProtein BindingProtein TransportAntimicrobial Cationic PeptidesCation Transport ProteinsFerroportinHAMP protein, humanHepcidinsMutant Proteins

Identifiers

PMID19150361
PMCPMC2677177
OpenAlexW1997633964

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.