Evidence map›Paper›PMID 34274435›Full record

ArticleNeuroscience letters2021

CLN3, at the crossroads of endocytic trafficking.

Susan L Cotman, Stéphane Lefrancois

Open access · greenAbstract read
In one paragraph

Article in Neuroscience letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Yeast as a Model for Human Disease.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Molecular syndromology · 2023
    Article
  14. Article
  15. Article
  16. Autophagy in the Neuronal Ceroid Lipofuscinoses (Batten Disease).Frontiers in cell and developmental biology · 2022
    Review
  17. 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

2 authors at 2 institutions in 2 countries.

Susan L CotmanCenter for Genomic Medicine, Department of Neurology, Mass General Research Institute, Massachusetts General Hospital, 185 Cambridge St., Boston, MA 02114, United States. Electronic address: scotman@mgh.harvard.edu.
Stéphane LefrancoisCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique, Laval H7V 1B7, Canada; Department of Anatomy and Cell Biology, McGill University, Montreal H3A 0C7, Canada; Centre d'Excellence en Recherche sur les Maladies Orphelines - Fondation Courtois (CERMO-FC), Université du Québec à Montréal (UQAM), Montréal H2X 3Y7, Canada. Electronic address: Stephane.Lefrancois@inrs.ca.
Massachusetts General Hospital · USUniversité du Québec à Montréal · CA

Funding

Modifiers of CLN3 diseaseR56NS113891 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI COTMAN, SUSAN LYNN · 2020 to 2020
$400k
CIHR ENG-155186NINDS NIH HHS R56 NS113891
6 · The paper itself

Abstract

The CLN3 gene was identified over two decades ago, but the primary function of the CLN3 protein remains unknown. Recessive inheritance of loss of function mutations in CLN3 are responsible for juvenile neuronal ceroid lipofuscinosis (Batten disease, or CLN3 disease), a fatal childhood onset neurodegenerative disease causing vision loss, seizures, progressive dementia, motor function loss and premature death. CLN3 is a multipass transmembrane protein that primarily localizes to endosomes and lysosomes. Defects in endocytosis, autophagy, and lysosomal function are common findings in CLN3-deficiency model systems. However, the molecular mechanisms underlying these defects have not yet been fully elucidated. In this mini-review, we will summarize the current understanding of the CLN3 protein interaction network and discuss how this knowledge is starting to delineate the molecular pathogenesis of CLN3 disease. Accumulating evidence strongly points towards CLN3 playing a role in regulation of the cytoskeleton and cytoskeletal associated proteins to tether cellular membranes, regulation of membrane complexes such as channels/transporters, and modulating the function of small GTPases to effectively mediate vesicular movement and membrane dynamics.

Indexed as

AnimalsEndosomesHumansLysosomesMembrane GlycoproteinsMolecular ChaperonesMutationNeuronal Ceroid-LipofuscinosesProtein TransportCLN3 protein, humanMembrane GlycoproteinsMolecular ChaperonesActinAutophagyCLN3CytoskeletonEndocytosisIntracellular traffickingIon channels

Identifiers

PMID34274435
PMCPMC8435016
OpenAlexW3184605030

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.