Evidence map›Paper›PMID 28100687›Full record

ArticleThe Journal of cell biology2017

A STRIPAK complex mediates axonal transport of autophagosomes and dense core vesicles through PP2A regulation.

Amanda L Neisch, Thomas P Neufeld, Thomas S Hays

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.

  1. Guideline
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  8. AnalysisbioRxiv : the preprint server for biology · 2025
    Article
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  10. Review
  11. Article
  12. Article
  13. Review
  14. STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  15. Article
  16. Article
  17. Review
  18. Article
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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

3 authors at 1 institution in 1 country.

Amanda L NeischDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455.ORCID http://orcid.org/0000-0002-3002-9221
Thomas P NeufeldDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455.
Thomas S HaysDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455 haysx001@umn.edu.ORCID http://orcid.org/0000-0002-4911-6042
University of Minnesota · US

Funding

STRUCTURE AND FUNCTION OF CYTOPLASMIC DYNEINR01GM044757 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HAYS, THOMAS S · 1990 to 2022
$5.7M
Regulation of TOR Signaling and Autophagy in DrosophilaR01GM062509 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI NEUFELD, THOMAS P. · 2001 to 2013
$3.8M
American Heart Association-American Stroke Association 15POST22790015NIGMS NIH HHS R01 GM044757NIGMS NIH HHS R01 GM062509
6 · The paper itself

Abstract

Autophagy plays an essential role in the cellular homeostasis of neurons, facilitating the clearance of cellular debris. This clearance process is orchestrated through the assembly, transport, and fusion of autophagosomes with lysosomes for degradation. The motor protein dynein drives autophagosome motility from distal sites of assembly to sites of lysosomal fusion. In this study, we identify the scaffold protein CKA (connector of kinase to AP-1) as essential for autophagosome transport in neurons. Together with other core components of the striatin-interacting phosphatase and kinase (STRIPAK) complex, we show that CKA associates with dynein and directly binds Atg8a, an autophagosomal protein. CKA is a regulatory subunit of PP2A, a component of the STRIPAK complex. We propose that the STRIPAK complex modulates dynein activity. Consistent with this hypothesis, we provide evidence that CKA facilitates axonal transport of dense core vesicles and autophagosomes in a PP2A-dependent fashion. In addition, CKA-deficient flies exhibit PP2A-dependent motor coordination defects. CKA function within the STRIPAK complex is crucial to prevent transport defects that may contribute to neurodegeneration.

Indexed as

Axonal TransportAdaptor Proteins, Signal TransducingAnimalsAnimals, Genetically ModifiedAutophagosomesAxonsCell LineDrosophila melanogasterDrosophila ProteinsDyneinsGenotypeMicroscopy, FluorescenceMultiprotein ComplexesMutationNerve Tissue ProteinsPhenotypeAdaptor Proteins, Signal TransducingAtg8a protein, DrosophilaCka protein, DrosophilaDrosophila ProteinsDyneinsMob4 protein, Drosophilamts protein, DrosophilaMultiprotein ComplexesNerve Tissue ProteinsProtein Phosphatase 2Recombinant Fusion Proteins

Identifiers

PMID28100687
PMCPMC5294782
OpenAlexW2576077292

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.