Evidence map›Paper›PMID 31801062›Full record

ArticleCell reports2019

Synaptic Kalirin-7 and Trio Interactomes Reveal a GEF Protein-Dependent Neuroligin-1 Mechanism of Action.

Jeremiah D Paskus, Chen Tian, Erin Fingleton, Christine Shen, Xiaobing Chen, Yan Li, Samuel A Myers, John D Badger, Michael A Bemben, Bruce E Herring and 1 more

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

Article in Cell reports, 2019. 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
2.0field-weighted citation impact, top 14% 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, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Cell Adhesion Molecule Signaling at the Synapse: Beyond the Scaffold.Cold Spring Harbor perspectives in biology · 2024
    Review
  6. Protein 4.1N Plays a Cell Type-Specific Role in Hippocampal Glutamatergic Synapse Regulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  7. Regulation of NLGN3 and the Synaptic Rho-GEF Signaling Pathway by CDK5.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  8. A Novel Cis-Regulatory lncRNA,Non-coding RNA · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Autism Spectrum Disorder/Intellectual Disability-Associated Mutations in Trio Disrupt Neuroligin 1-Mediated Synaptogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Advances in Proteomics Allow Insights Into Neuronal Proteomes.Frontiers in molecular neuroscience · 2021
    Review
  20. 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.

Jeremiah D PaskusReceptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD, USA; Interdisciplinary Program in Neuroscience, Georgetown University Medical Center, Washington, DC, USA.
Chen TianDepartment of Biological Sciences, University of Southern California, Los Angeles, CA, USA; Neuroscience Graduate Program, University of Southern California, Los Angeles, CA, USA.
Erin FingletonReceptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD, USA.
Christine ShenLaboratory of Neurobiology, NINDS, NIH, Bethesda, MD, USA.
Xiaobing ChenLaboratory of Neurobiology, NINDS, NIH, Bethesda, MD, USA.
Yan LiProtein/Peptide Sequencing Facility, NINDS, NIH, Bethesda, MD, USA.
Samuel A MyersThe Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
John D BadgerReceptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD, USA.
Michael A BembenReceptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD, USA; Department of Biology, The Johns Hopkins University, Baltimore, MD, USA.
Bruce E HerringDepartment of Biological Sciences, University of Southern California, Los Angeles, CA, USA. Electronic address: bherring@usc.edu.
Katherine W RocheReceptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD, USA. Electronic address: rochek@ninds.nih.gov.
National Institute of Neurological Disorders and Stroke · USUniversity of Southern California · USBroad Institute · USGeorgetown University · USNational Institutes of Health · US

Funding

Predoctoral Training in Intergrative NeuroscienceT32NS041231 · NINDS · GEORGETOWN UNIVERSITY · PI Ludise Malkova, Ashley S VanMeter · 2001 to 2026
$6.8M
Uncovering the Role of TRIO in Synaptic Function and Autism Spectrum DisorderR01NS112480 · NINDS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HERRING, BRUCE · 2019 to 2023
$1.8M
Kalirin-7's role in synaptic transmission, plasticity and learning and memoryR00MH103398 · NIMH · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HERRING, BRUCE · 2016 to 2018
$730k
Kalirin-7's role in synaptic transmission, plasticity and learning and memoryK99MH103398 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HERRING, BRUCE · 2014 to 2015
$176k
NIMH NIH HHS K99 MH103398NIMH NIH HHS R00 MH103398NINDS NIH HHS R01 NS112480NINDS NIH HHS T32 NS041231
6 · The paper itself

Abstract

The RhoGEFs Kalirin-7 and Trio are regulators of synaptic plasticity, and their dysregulation is associated with a range of neurodevelopmental and neurodegenerative disorders. Although studies have implicated both Kalirin and Trio in certain diseases, such as tauopathies, they remarkably differ in their association with other disorders. Using unbiased proteomics, we identified interactomes of Kalirin-7 and Trio to ascertain distinct protein association networks associated with their respective function and revealed groups of proteins that preferentially interact with a particular RhoGEF. In comparison, we find Trio interacts with a range of axon guidance and presynaptic complexes, whereas Kalirin-7 associates with several synaptic adhesion molecules. Specifically, we show Kalirin-7 is an interactor of the cell adhesion molecule neuroligin-1 (NLGN1), and NLGN1-dependent synaptic function is mediated through Kalirin-7 in an interaction-dependent manner. Our data reveal not only the interactomes of two important disease-related proteins, but also provide an intracellular effector of NLGN1 function.

Indexed as

AnimalsCell Adhesion Molecules, NeuronalCell LineFemaleGuanine Nucleotide Exchange FactorsHEK293 CellsHumansMaleMiceMice, Inbred C57BLProtein Serine-Threonine KinasesRats, Sprague-DawleyRho Guanine Nucleotide Exchange FactorsSynapsesCell Adhesion Molecules, NeuronalGuanine Nucleotide Exchange FactorsKALRN protein, humanneuroligin 1Protein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsTRIO protein, humankalirinneuroliginproteomicssynaptic transmissionsynaptogenesisTrio

Identifiers

PMID31801062
PMCPMC9012321
OpenAlexW2994046146

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.