Evidence map›Paper›PMID 27555448›Full record

ArticleNature communications2016

Temporal regulation of Lsp1 O-GlcNAcylation and phosphorylation during apoptosis of activated B cells.

Jung-Lin Wu, Hsin-Yi Wu, Dong-Yan Tsai, Ming-Feng Chiang, Yi-Ju Chen, Shijay Gao, Chun-Cheng Lin, Chun-Hung Lin, Kay-Hooi Khoo, Yu-Ju Chen and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.Journal of the American Chemical Society · 2024
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. O-Linked β-Frontiers in immunology · 2022
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  20. O-GlcNAcylation and its role in the immune system.Journal of biomedical science · 2020
    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

11 authors at 5 institutions in 1 country.

Jung-Lin WuInstitute of Microbiology and Immunology, National Yang-Ming University, Taipei 112, Taiwan.ORCID 0000-0003-1054-9016
Hsin-Yi WuInstitute of Chemistry, Academia Sinica, Taipei 115, Taiwan.
Dong-Yan TsaiGenomics Research Center, Academia Sinica, Taipei 115, Taiwan.
Ming-Feng ChiangGenomics Research Center, Academia Sinica, Taipei 115, Taiwan.
Yi-Ju ChenInstitute of Chemistry, Academia Sinica, Taipei 115, Taiwan.
Shijay GaoInstitute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
Chun-Cheng LinDepartment of Chemistry, National Tsing Hua University, Hsinchu 300, Taiwan.
Chun-Hung LinInstitute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
Kay-Hooi KhooInstitute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
Yu-Ju ChenInstitute of Chemistry, Academia Sinica, Taipei 115, Taiwan.
Kuo-I LinGenomics Research Center, Academia Sinica, Taipei 115, Taiwan.
Institute of Chemistry, Academia Sinica · TWGenomics Research Center, Academia Sinica · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Tsing Hua University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crosslinking of B-cell receptor (BCR) sets off an apoptosis programme, but the underlying pathways remain obscure. Here we decipher the molecular mechanisms bridging B-cell activation and apoptosis mediated by post-translational modification (PTM). We find that O-GlcNAcase inhibition enhances B-cell activation and apoptosis induced by BCR crosslinking. This proteome-scale analysis of the functional interplay between protein O-GlcNAcylation and phosphorylation in stimulated mouse primary B cells identifies 313 O-GlcNAcylation-dependent phosphosites on 224 phosphoproteins. Among these phosphoproteins, temporal regulation of the O-GlcNAcylation and phosphorylation of lymphocyte-specific protein-1 (Lsp1) is a key switch that triggers apoptosis in activated B cells. O-GlcNAcylation at S209 of Lsp1 is a prerequisite for the recruitment of its kinase, PKC-β1, to induce S243 phosphorylation, leading to ERK activation and downregulation of BCL-2 and BCL-xL. Thus, we demonstrate the critical PTM interplay of Lsp1 that transmits signals for initiating apoptosis after BCR ligation.

Indexed as

AcetylglucosamineAnimalsApoptosisbeta-N-AcetylhexosaminidasesB-LymphocytesCalcium-Binding ProteinsEnzyme InhibitorsGlycosylationLymphocyte ActivationMiceMice, Inbred C57BLMicrofilament ProteinsPhosphorylationProtein Kinase C betaPyransSignal TransductionAcetylglucosaminebeta-N-AcetylhexosaminidasesCalcium-Binding ProteinsEnzyme Inhibitorshexosaminidase CLsp1 protein, mouseMicrofilament ProteinsProtein Kinase C betaPyransthiamet GThiazoles

Identifiers

PMID27555448
PMCPMC4999498
OpenAlexW2515797086

What OpenQuestion holds

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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.