Evidence map›Paper›PMID 32482796›Full record

ArticleJournal of cell science2020

The DISC1-Girdin complex - a missing link in signaling to the T cell cytoskeleton.

Nicholas Maskalenko, Shubhankar Nath, Adarsh Ramakrishnan, Nadia Anikeeva, Yuri Sykulev, Martin Poenie

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. 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

6 authors at 2 institutions in 1 country.

Nicholas MaskalenkoMolecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.ORCID 0000-0001-7690-5234
Shubhankar NathCellink LLC, 100 Franklin St., Boston, MA 02110, USA.ORCID 0000-0001-5778-7615
Adarsh RamakrishnanMolecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.ORCID 0000-0002-2922-5778
Nadia AnikeevaDepartment of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0003-1494-6270
Yuri SykulevDepartment of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0002-9685-0223
Martin PoenieMolecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA poenie@austin.utexas.edu.ORCID 0000-0003-2524-4039
The University of Texas at Austin · USThomas Jefferson University · US

Funding

Viral control mechanisms of HIV-specific T cells in HIV-infected lymph nodeR01AI118694 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI BETTS, MICHAEL R · 2015 to 2019
$3.3M
NIAID NIH HHS R01 AI118694
6 · The paper itself

Abstract

In this study, using Jurkat cells, we show that DISC1 (disrupted in schizophrenia 1) and Girdin (girders of actin filament) are essential for typical actin accumulation at the immunological synapse. Furthermore, DISC1, Girdin and dynein are bound in a complex. Although this complex initially forms as a central patch at the synapse, it relocates to a peripheral ring corresponding to the peripheral supramolecular activation cluster (pSMAC). In the absence of DISC1, the classic actin ring does not form, cell spreading is blocked, and the dynein complex fails to relocate to the pSMAC. A similar effect is seen when Girdin is deleted. When cells are treated with inhibitors of actin polymerization, the dynein-NDE1 complex is lost from the synapse and the microtubule-organizing center fails to translocate, suggesting that actin and dynein might be linked. Upon stimulation of T cell receptors, DISC1 becomes associated with talin, which likely explains why the dynein complex colocalizes with the pSMAC. These results show that the DISC1-Girdin complex regulates actin accumulation, cell spreading and distribution of the dynein complex at the synapse.This article has an associated First Person interview with the first author of the paper.

Indexed as

CytoskeletonMicrotubulesActinsHumansImmunological SynapsesMicrotubule-Associated ProteinsNerve Tissue ProteinsSignal TransductionActinsDISC1 protein, humanMicrotubule-Associated ProteinsNde1 protein, humanNerve Tissue ProteinsActin dynamicsDISC1DyneinGirdinImmunological synapse

Identifiers

PMID32482796
PMCPMC7358132
OpenAlexW3031004635

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.