Evidence map›Paper›PMID 31221560›Full record

ArticleNeuron2019

Neuronally Enriched RUFY3 Is Required for Caspase-Mediated Axon Degeneration.

Nicholas T Hertz, Eliza L Adams, Ross A Weber, Rebecca J Shen, Melanie K O'Rourke, David J Simon, Henry Zebroski, Olav Olsen, Charles W Morgan, Trevor R Mileur and 7 more

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

Article in Neuron, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. An atlas of caspase cleavage events in differentiating muscle cells.Protein science : a publication of the Protein Society · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Non-Canonical Roles of Apoptotic Caspases in the Nervous System.Frontiers in cell and developmental biology · 2022
    Review
  8. Article
  9. Cell Death Related Proteins Beyond Apoptosis in the CNS.Frontiers in cell and developmental biology · 2021
    Review
  10. Review
  11. Review
  12. 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

17 authors at 3 institutions in 1 country.

Nicholas T HertzDepartment of Biology, Stanford University, Stanford, CA, USA; Laboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA.
Eliza L AdamsDepartment of Biology, Stanford University, Stanford, CA, USA; Laboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA.
Ross A WeberLaboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA.
Rebecca J ShenDepartment of Biology, Stanford University, Stanford, CA, USA.
Melanie K O'RourkeDepartment of Biology, Stanford University, Stanford, CA, USA.
David J SimonDepartment of Biology, Stanford University, Stanford, CA, USA; Laboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA.
Henry ZebroskiProteomics Resource Center, The Rockefeller University, New York, NY, USA.
Olav OlsenLaboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA.
Charles W MorganDepartments of Pharmaceutical Chemistry and Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA, USA.
Trevor R MileurDepartment of Biology, Stanford University, Stanford, CA, USA.
Angela M HitchcockDepartment of Biology, Stanford University, Stanford, CA, USA.
Nicholas A Sinnott ArmstrongDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, USA.
Michael WainbergDepartment of Computer Science, Stanford University School of Engineering, Stanford, CA, USA.
Michael C BassikDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, USA.
Henrik MolinaProteomics Resource Center, The Rockefeller University, New York, NY, USA.
James A WellsDepartments of Pharmaceutical Chemistry and Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA, USA.
Marc Tessier-LavigneDepartment of Biology, Stanford University, Stanford, CA, USA; Laboratory of Brain Development and Repair, The Rockefeller University, New York, NY, USA. Electronic address: tessier3@stanford.edu.
Rockefeller University · USStanford University · USUniversity of California, San Francisco · US

Funding

Training Program in Basic NeuroscienceT32MH020016 · NIMH · STANFORD UNIVERSITY · PI Justin L Gardner, Merritt C Maduke · 1997 to 2026
$16.2M
Global Analysis of Proteolysis in ApoptosisR01GM081051 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2007 to 2015
$2.8M
Regulation of axon degeneration by the apoptotic pathwayR01NS089786 · NINDS · STANFORD UNIVERSITY · PI TESSIER-LAVIGNE, MARC · 2014 to 2018
$2.8M
Affinity-directed tagging of protein binding partners in signalingR01CA191018 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2014 to 2018
$1.6M
NCI NIH HHS R01 CA191018NIGMS NIH HHS R01 GM081051NIMH NIH HHS T32 MH020016NINDS NIH HHS R01 NS089786
6 · The paper itself

Abstract

Selective synaptic and axonal degeneration are critical aspects of both brain development and neurodegenerative disease. Inhibition of caspase signaling in neurons is a potential therapeutic strategy for neurodegenerative disease, but no neuron-specific modulators of caspase signaling have been described. Using a mass spectrometry approach, we discovered that RUFY3, a neuronally enriched protein, is essential for caspase-mediated degeneration of TRKA+ sensory axons in vitro and in vivo. Deletion of Rufy3 protects axons from degeneration, even in the presence of activated CASP3 that is competent to cleave endogenous substrates. Dephosphorylation of RUFY3 at residue S34 appears required for axon degeneration, providing a potential mechanism for neurons to locally control caspase-driven degeneration. Neuronally enriched RUFY3 thus provides an entry point for understanding non-apoptotic functions of CASP3 and a potential target to modulate caspase signaling specifically in neurons for neurodegenerative disease.

Indexed as

AnimalsAxonsCaspase 3Cells, CulturedCytoskeletal ProteinsEnzyme ActivationGanglia, SpinalMiceMice, KnockoutNerve DegenerationNerve Tissue ProteinsPhosphorylationProtein Processing, Post-TranslationalReceptor, trkASensory Receptor CellsStructure-Activity RelationshipCasp3 protein, mouseCaspase 3Cytoskeletal ProteinsNerve Tissue ProteinsReceptor, trkARufy3 protein, mouseaxon degenerationcaspase signalingchemical biologydegradomicsmass spectrometryneurodegeneration

Identifiers

PMID31221560
PMCPMC8024238
OpenAlexW2953080219

What OpenQuestion holds

Textmetadata
LicenceTDM
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.