Evidence map›Paper›PMID 25586186›Full record

ArticleThe Journal of biological chemistry2015

Scaffold protein JLP is critical for CD40 signaling in B lymphocytes.

Hui-ming Wang, Qi Yan, Tao Yang, Hui Cheng, Juan Du, Katsuji Yoshioka, Sam K P Kung, Guo-hua Ding

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Anti-CD40 Antibodies Fused to CD40 Ligand Have Superagonist Properties.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Observational
  13. Article
  14. Ciliobrevins as tools for studying dynein motor function.Frontiers in cellular neuroscience · 2015
    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

8 authors at 3 institutions in 3 countries.

Hui-ming WangFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China, wanghuimingwhm@yahoo.com.
Qi YanFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.
Tao YangFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.
Hui ChengFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.
Juan DuFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.
Katsuji Yoshiokathe Division of Molecular Cell Signaling, Department of Molecular and Cellular Biology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan.
Sam K P Kungthe Department of Immunology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada, and.
Guo-hua DingFrom the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China, ghxding@gmail.com.
Wuhan University · CNKanazawa University · JPUniversity of Manitoba · CA

Funding

Canadian Institutes of Health Research 109761
6 · The paper itself

Abstract

CD40 expression on the surface of B lymphocytes is essential for their biological function and fate decision. The engagement of CD40 with its cognate ligand, CD154, leads to a sequence of cellular events in B lymphocytes, including CD40 cytoplasmic translocation, a temporal and spatial organization of effector molecules, and a cascade of CD40-induced signal transduction. The JLP scaffold protein was expressed in murine B lymphocytes. Using B lymphocytes from jlp-deficient mice, we observed that JLP deficiency resulted in defective CD40 internalization upon CD154/CD40 engagement. Examination of interactions and co-localization among CD40, JLP, dynein, and Rab5 in B lymphocytes suggested that CD40 internalization is a process of JLP-mediated vesicle transportation that depends on Rab5 and dynein. JLP deficiency also diminished CD40-dependent activation of MAPK and JNK, but not NF-κB. Inhibiting vesicle transportation from the direction of cell periphery to the cell center by a dynein inhibitor (ciliobrevin D) impaired both CD154-induced CD40 internalization and CD40-dependent MAPK activities in B lymphocytes. Collectively, our data demonstrate a novel role of the JLP scaffold protein in the bridging of CD154-triggered CD40 internalization and CD40-dependent signaling in splenic B lymphocytes.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingAnimalsBlotting, WesternB-LymphocytesCD40 AntigensCD40 LigandCells, CulturedDyneinsEndocytosisFemaleFlow CytometryHEK293 CellsHumansJNK Mitogen-Activated Protein KinasesMaleAdaptor Proteins, Signal TransducingCD40 AntigensCD40 LigandDyneinsJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinasesrab5 GTP-Binding ProteinsSpag9 protein, mouseCell SignalingMitogen-activated Protein Kinase (MAPK)ReceptorScaffold ProteinTrafficking

Identifiers

PMID25586186
PMCPMC4342446
OpenAlexW2059812027

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.