Evidence map›Paper›PMID 24872409›Full record

ArticleThe Journal of biological chemistry2014

Phosphorylation of Rab5a protein by protein kinase Cϵ is crucial for T-cell migration.

Seow Theng Ong, Michael Freeley, Joanna Skubis-Zegadło, Mobashar Hussain Urf Turabe Fazil, Dermot Kelleher, Friedrich Fresser, Gottfried Baier, Navin Kumar Verma, Aideen Long

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  6. β2 Integrins-Multi-Functional Leukocyte Receptors in Health and Disease.International journal of molecular sciences · 2020
    Review
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  19. Article
  20. Rab-mediated vesicle trafficking in cancer.Journal of biomedical science · 2016
    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

9 authors at 4 institutions in 5 countries.

Seow Theng OngFrom the From the Department of Clinical Medicine, Institute of Molecular Medicine, Trinity College Dublin, Dublin 8, Ireland.
Michael FreeleyFrom the From the Department of Clinical Medicine, Institute of Molecular Medicine, Trinity College Dublin, Dublin 8, Ireland.
Joanna Skubis-ZegadłoFrom the From the Department of Clinical Medicine, Institute of Molecular Medicine, Trinity College Dublin, Dublin 8, Ireland, Department of Applied Pharmacy and Bioengineering, Medical University of Warsaw, 02-091 Warsaw, Poland.
Mobashar Hussain Urf Turabe FazilLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 637553.
Dermot KelleherLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 637553, Faculty of Medicine, Imperial College London, Exhibition Road, London SW7 2AZ, United Kingdom, and.
Friedrich Fresserthe Department of Medical Genetics, Molecular and Clinical Pharmacology, Innsbruck Medical University, A-6020 Innsbruck, Austria.
Gottfried Baierthe Department of Medical Genetics, Molecular and Clinical Pharmacology, Innsbruck Medical University, A-6020 Innsbruck, Austria.
Navin Kumar VermaLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 637553, nkverma@ntu.edu.sg.
Aideen LongFrom the From the Department of Clinical Medicine, Institute of Molecular Medicine, Trinity College Dublin, Dublin 8, Ireland, longai@tcd.ie.
Nanyang Technological University · SGTrinity College Dublin · IEInnsbruck Medical University · ATMedical University of Warsaw · PL

Funding

Austrian Science Fund FWF P 25044
6 · The paper itself

Abstract

Rab GTPases control membrane traffic and receptor-mediated endocytosis. Within this context, Rab5a plays an important role in the spatial regulation of intracellular transport and signal transduction processes. Here, we report a previously uncharacterized role for Rab5a in the regulation of T-cell motility. We show that Rab5a physically associates with protein kinase Cϵ (PKCϵ) in migrating T-cells. After stimulation of T-cells through the integrin LFA-1 or the chemokine receptor CXCR4, Rab5a is phosphorylated on an N-terminal Thr-7 site by PKCϵ. Both Rab5a and PKCϵ dynamically interact at the centrosomal region of migrating cells, and PKCϵ-mediated phosphorylation on Thr-7 regulates Rab5a trafficking to the cell leading edge. Furthermore, we demonstrate that Rab5a Thr-7 phosphorylation is functionally necessary for Rac1 activation, actin rearrangement, and T-cell motility. We present a novel mechanism by which a PKCϵ-Rab5a-Rac1 axis regulates cytoskeleton remodeling and T-cell migration, both of which are central for the adaptive immune response.

Indexed as

Adaptive ImmunityCell LineCell MovementCytoskeletonFemaleHumansLymphocyte Function-Associated Antigen-1MalePhosphorylationProtein Kinase C-epsilonrab5 GTP-Binding ProteinsReceptors, CXCR4T-LymphocytesCXCR4 protein, humanLymphocyte Function-Associated Antigen-1PRKCE protein, humanProtein Kinase C-epsilonrab5 GTP-Binding ProteinsReceptors, CXCR4Cell MigrationCell SignalingImmunologyIntegrinPhosphorylationRab ProteinsSignal TransductionT-cell

Identifiers

PMID24872409
PMCPMC4094053
OpenAlexW2049083762

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.