Evidence map›Paper›PMID 25336657›Full record

ArticleThe Journal of biological chemistry2014

FBXO22 protein is required for optimal synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine.

Elena Dikopoltsev, Veronika N Foltyn, Martin Zehl, Ole N Jensen, Hisashi Mori, Inna Radzishevsky, Herman Wolosker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Energy Landscape of Human Serine Racemase.Frontiers in molecular biosciences · 2018
    Review
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  9. Article
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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

7 authors at 2 institutions in 2 countries.

Elena DikopoltsevFrom the Department of Biochemistry, Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 31096, Israel.
Veronika N FoltynFrom the Department of Biochemistry, Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 31096, Israel.
Martin Zehlthe Department of Pharmacognosy, University of Vienna, 1090 Vienna, Austria.
Ole N Jensenthe Department of Biochemistry and Molecular Biology, University of Southern Denmark, 5230 Odense M, Denmark, and.
Hisashi Morithe Department of Molecular Neuroscience, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan.
Inna RadzishevskyFrom the Department of Biochemistry, Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 31096, Israel.
Herman WoloskerFrom the Department of Biochemistry, Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 31096, Israel, hwolosker@tx.technion.ac.il.
University of Toyama · JPUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

d-Serine is a physiological activator of NMDA receptors (NMDARs) in the nervous system that mediates several NMDAR-mediated processes ranging from normal neurotransmission to neurodegeneration. d-Serine is synthesized from l-serine by serine racemase (SR), a brain-enriched enzyme. However, little is known about the regulation of d-serine synthesis. We now demonstrate that the F-box only protein 22 (FBXO22) interacts with SR and is required for optimal d-serine synthesis in cells. Although FBXO22 is classically associated with the ubiquitin system and is recruited to the Skip1-Cul1-F-box E3 complex, SR interacts preferentially with free FBXO22 species. In vivo ubiquitination and SR half-life determination indicate that FBXO22 does not target SR to the proteasome system. FBXO22 primarily affects SR subcellular localization and seems to increase d-serine synthesis by preventing the association of SR to intracellular membranes. Our data highlight an atypical role of FBXO22 in enhancing d-serine synthesis that is unrelated to its classical effects as a component of the ubiquitin-proteasome degradation pathway.

Indexed as

Cell Line, TumorEscherichia coliF-Box ProteinsGene Expression RegulationHalf-LifeHumansIntracellular MembranesNeurogliaNeuronsProteasome Endopeptidase ComplexProteolysisRacemases and EpimerasesReceptors, Cytoplasmic and NuclearReceptors, N-Methyl-D-AspartateRecombinant ProteinsRNA, Small InterferingF-Box ProteinsFBXO22 protein, humanProteasome Endopeptidase ComplexRacemases and EpimerasesReceptors, Cytoplasmic and NuclearReceptors, N-Methyl-D-AspartateRecombinant ProteinsRNA, Small InterferingSerineSerine Racemased-SerineF-box ProteinsFBXO22Glutamate ReceptorNeurotransmitterNeurotransmitter ReceptorNMDA ReceptorSerine RacemaseUbiquitinUbiquitylation (Ubiquitination)

Identifiers

PMID25336657
PMCPMC4256329
OpenAlexW2026443912

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.