Evidence map›Paper›PMID 20529854›Full record

ArticleThe Journal of biological chemistry2010

Binding of cysteine synthase to the STAS domain of sulfate transporter and its regulatory consequences.

Nakako Shibagaki, Arthur R Grossman

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Inorganic sulfate is critical forProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Hydrogen sulfide (HaBIOTECH · 2021
    Review
  14. Genome-Wide Identification of Sultr Genes inFrontiers in plant science · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Nakako ShibagakiDepartment of Plant Biology, The Carnegie Institution for Science, Stanford, California 94305, USA. nshibagaki@mls.eng.osaka-u.ac.jp
Arthur R Grossman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sulfate ion (SO(4)(2-)) is transported into plant root cells by SO(4)(2-) transporters and then mostly reduced to sulfide (S(2-)). The S(2-) is then bonded to O-acetylserine through the activity of cysteine synthase (O-acetylserine (thiol)lyase or OASTL) to form cysteine, the first organic molecule of the SO(4)(2-) assimilation pathway. Here, we show that a root plasma membrane SO(4)(2-) transporter of Arabidopsis, SULTR1;2, physically interacts with OASTL. The interaction was initially demonstrated using a yeast two-hybrid system and corroborated by both in vivo and in vitro binding assays. The domain of SULTR1;2 shown to be important for association with OASTL is called the STAS domain. This domain is at the C terminus of the transporter and extends from the plasma membrane into the cytoplasm. The functional relevance of the OASTL-STAS interaction was investigated using yeast mutant cells devoid of endogenous SO(4)(2-) uptake activity but co-expressing SULTR1;2 and OASTL. The analysis of SO(4)(2-) transport in these cells suggests that the binding of OASTL to the STAS domain in this heterologous system negatively impacts transporter activity. In contrast, the activity of purified OASTL measured in vitro was enhanced by co-incubation with the STAS domain of SULTR1;2 but not with the analogous domain of the SO(4)(2-) transporter isoform SULTR1;1, even though the SULTR1;1 STAS peptide also interacts with OASTL based on the yeast two-hybrid system and in vitro binding assays. These observations suggest a regulatory model in which interactions between SULTR1;2 and OASTL coordinate internalization of SO(4)(2-) with the energetic/metabolic state of plant root cells.

Indexed as

Anion Transport ProteinsArabidopsisArabidopsis ProteinsCell MembraneMicroscopy, FluorescenceMicrosomesModels, BiologicalPlant RootsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSulfatesSulfurTwo-Hybrid System TechniquesAnion Transport ProteinsArabidopsis ProteinsSulfatesSulfurSultr1;2 protein, Arabidopsis

Identifiers

PMID20529854
PMCPMC2915745

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.