Evidence map›Paper›PMID 21987636›Full record

ArticleThe Journal of cell biology2011

The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly.

Rachel Kama, Vydehi Kanneganti, Christian Ungermann, Jeffrey E Gerst

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-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

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. Yeast as a Model for Human Disease.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Autophagy in the Neuronal Ceroid Lipofuscinoses (Batten Disease).Frontiers in cell and developmental biology · 2022
    Review
  6. Review
  7. Altered protein secretion in Batten disease.Disease models & mechanisms · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Cellular models of Batten disease.Biochimica et biophysica acta. Molecular basis of disease · 2020
    Review
  12. The CLN3 gene and protein: What we know.Molecular genetics & genomic medicine · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Vision loss in juvenile neuronal ceroid lipofuscinosis (CLN3 disease).Annals of the New York Academy of Sciences · 2016
    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

4 authors at 2 institutions in 2 countries.

Rachel KamaDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Vydehi Kanneganti
Christian Ungermann
Jeffrey E Gerst
Weizmann Institute of Science · ILOsnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human Batten disease gene CLN3 and yeast orthologue BTN1 encode proteins of unclear function. We show that the loss of BTN1 phenocopies that of BTN2, which encodes a retromer accessory protein involved in the retrieval of specific cargo from late endosomes (LEs) to the Golgi. However, Btn1 localizes to Golgi and regulates soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor (SNARE) function to control retrograde transport. Specifically, BTN1 overexpression and deletion have opposing effects on phosphorylation of the Sed5 target membrane SNARE, on Golgi SNARE assembly, and on Golgi integrity. Although Btn1 does not interact physically with SNAREs, it regulates Sed5 phosphorylation by modulating Yck3, a palmitoylated endosomal kinase. This may involve modification of the Yck3 lipid anchor, as substitution with a transmembrane domain suppresses the deletion of BTN1 and restores trafficking. Correspondingly, deletion of YCK3 mimics that of BTN1 or BTN2 with respect to LE-Golgi retrieval. Thus, Btn1 controls retrograde sorting by regulating SNARE phosphorylation and assembly, a process that may be adversely affected in Batten Disease patients.

Indexed as

Protein TransportButyrophilinsCasein Kinase IEndosomesGolgi ApparatusHumansMembrane GlycoproteinsMolecular ChaperonesNeuronal Ceroid-LipofuscinosesPhosphorylationSaccharomyces cerevisiae ProteinsSNARE ProteinsYeastsButyrophilinsCasein Kinase ICLN3 protein, humanMembrane GlycoproteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSNARE ProteinsYCK3 protein, S cerevisiae

Identifiers

PMID21987636
PMCPMC3198160
OpenAlexW1975545686

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.