Evidence map›Paper›PMID 24328790›Full record

ArticleThe Biochemical journal2014

Phosphorylation of Arabidopsis transketolase at Ser428 provides a potential paradigm for the metabolic control of chloroplast carbon metabolism.

Agostinho G Rocha, Norbert Mehlmer, Simon Stael, Andrea Mair, Nargis Parvin, Fatima Chigri, Markus Teige, Ute C Vothknecht

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2014. 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
2.1field-weighted citation impact, top 13% 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, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Uridylation and the SKI complex orchestrate the Calvin cycle of photosynthesis through RNA surveillance ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. The Significance of Calcium in Photosynthesis.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. 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

8 authors at 4 institutions in 2 countries.

Agostinho G Rocha*Department of Biology I, LMU Munich, Groβhaderner Str. 2-4, D-82152 Planegg-Martinsried, Germany.
Norbert Mehlmer*Department of Biology I, LMU Munich, Groβhaderner Str. 2-4, D-82152 Planegg-Martinsried, Germany.
Simon Stael†Department of Biochemistry, MFPL, University of Vienna, Dr. Bohr Gasse 9/5, A-1030 Vienna, Austria.
Andrea Mair‡Department of Molecular Systems Biology (MoSys), University of Vienna, Althanstr. 14, A-1090 Vienna, Austria.
Nargis Parvin*Department of Biology I, LMU Munich, Groβhaderner Str. 2-4, D-82152 Planegg-Martinsried, Germany.
Fatima Chigri§Center for Integrated Protein Science (Munich), Department of Biology, LMU Munich, D-82152 Martinsried, Germany.
Markus Teige
Ute C Vothknecht
Ludwig-Maximilians-Universität München · DEUniversity of Vienna · ATCenter for Integrated Protein Science Munich · DEUrologische Klinik München · DE

Funding

Austrian Science Fund FWF P 25359
6 · The paper itself

Abstract

Calcium is an important second messenger in eukaryotic cells that regulates many different cellular processes. To elucidate calcium regulation in chloroplasts, we identified the targets of calcium-dependent phosphorylation within the stromal proteome. A 73 kDa protein was identified as one of the most dominant proteins undergoing phosphorylation in a calcium-dependent manner in the stromal extracts of both Arabidopsis and Pisum. It was identified as TKL (transketolase), an essential enzyme of both the Calvin-Benson-Bassham cycle and the oxidative pentose phosphate pathway. Calcium-dependent phosphorylation of both Arabidopsis isoforms (AtTKL1 and AtTKL2) could be confirmed in vitro using recombinant proteins. The phosphorylation is catalysed by a stroma-localized protein kinase, which cannot utilize GTP. Phosphorylation of AtTKL1, the dominant isoform in most tissues, occurs at a serine residue that is conserved in TKLs of vascular plants. By contrast, an aspartate residue is present in this position in cyanobacteria, algae and mosses. Characterization of a phosphomimetic mutant (S428D) indicated that Ser428 phosphorylation exerts significant effects on the enzyme's substrate saturation kinetics at specific physiological pH values. The results of the present study point to a role for TKL phosphorylation in the regulation of carbon allocation.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCarbonChloroplastsMolecular Sequence DataPhosphorylationProtein IsoformsSerineTransketolaseArabidopsis ProteinsCarbonProtein IsoformsSerineTransketolase

Identifiers

PMID24328790
PMCPMC3966265
OpenAlexW1989642230

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.