Evidence map›Paper›PMID 20348389›Full record

ArticleEukaryotic cell2010

Analysis of the high-affinity iron uptake system at the Chlamydomonas reinhardtii plasma membrane.

Alaina Terzulli, Daniel J Kosman

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Optimizing Fe Nutrition for Algal Growth.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Review
  6. Regulation of Iron Homeostasis and Use in Chloroplasts.International journal of molecular sciences · 2020
    Review
  7. Regulating cellular trace metal economy in algae.Current opinion in plant biology · 2017
    Review
  8. Article
  9. Article
  10. Iron economy in Chlamydomonas reinhardtii.Frontiers in plant science · 2013
    Review
  11. Review
  12. Article
  13. The ins and outs of algal metal transport.Biochimica et biophysica acta · 2012
    Review
  14. Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Disassembling iron availability to phytoplankton.Frontiers in microbiology · 2012
    Article
  16. Article
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.

Alaina TerzulliDepartment of Biochemistry, the University at Buffalo, 140 Farber Hall, 3435 Main St., Buffalo, NY 14214, USA.
Daniel J Kosman
University at Buffalo, State University of New York · US

Funding

Managing ionic iron: ferri-reduction, ferro-oxidation and iron permeationR01DK053820 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 1999 to 2016
$4.0M
Managing ionic iron: ferri-reduction, ferro-oxidation and iron permeationR56DK053820 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 2013 to 2013
$155k
NIDDK NIH HHS DK053820NIDDK NIH HHS R01 DK053820NIDDK NIH HHS R56 DK053820
6 · The paper itself

Abstract

Multicopper ferroxidases play a vital role in iron metabolism in bacteria, fungi, algae, and mammals. Saccharomyces cerevisiae utilizes a channeling mechanism to couple the ferroxidase activity of Fet3p to Fe(3+) transport into the cell by Ftr1p. In contrast, the mechanisms by which mammals couple the ferroxidase reaction to iron trafficking is unclear. The human ferroxidases ceruloplasmin and hephaestin are twice the size of Fet3p and interact with proteins that are not expressed in fungi. Chlamydomonas FOX1 is a homolog of the human ferroxidases but likely supports iron uptake in a manner similar to that of yeast, since Chlamydomonas reinhardtii expresses a ferric iron permease homolog, FTR1. The results presented support this hypothesis. We show that FOX1 is trafficked to the plasma membrane and is oriented with its multicopper oxidase/ferroxidase domain in the exocytoplasmic space. Our analysis of FTR1 indicates its topology is similar to that of S. cerevisiae Ftr1p, with a potential exocytoplasmic iron channeling motif and two potential iron permeation motifs in membrane-spanning regions. We demonstrate that high-affinity iron uptake is dependent on FOX1 and the copper status of the cell. Kinetic inhibition of high-affinity iron uptake by a ferric iron chelator does not reflect the strength of the chelator, supporting a ferric iron channeling mechanism for high-affinity iron uptake in Chlamydomonas. Last, recombinant FOX1 (rFOX1) has been isolated in a partially holo form that exhibits the UV-visible absorbance spectrum of a multicopper oxidase and the catalytic activity of a ferroxidase.

Indexed as

Algal ProteinsAmino Acid SequenceBiocatalysisCell LineCell MembraneCeruloplasminChlamydomonas reinhardtiiHumansIon TransportIronIron Chelating AgentsIron DeficienciesKineticsModels, BiologicalMolecular Sequence DataOxidoreductases Acting on CH-NH Group Donors4-phenylenediamine oxidaseAlgal ProteinsCeruloplasminIronIron Chelating AgentsOxidoreductases Acting on CH-NH Group DonorsTransferrin

Identifiers

PMID20348389
PMCPMC2863958
OpenAlexW2107249916

What OpenQuestion holds

Textmetadata
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.