Evidence map›Paper›PMID 23969831›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.

Jaerak Chang, Seongju Lee, Craig Blackstone

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.6field-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

43 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Visualizing ER-phagy and ER architecture in vivo.The Journal of cell biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Protrudin-mediated ER-endosome contact sites promote phagocytosis.Cellular and molecular life sciences : CMLS · 2023
    Article
  9. Article
  10. Review
  11. Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  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 2 institutions in 1 country.

Jaerak ChangCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Seongju Lee
Craig Blackstone
National Institutes of Health · USNational Institute of Neurological Disorders and Stroke · US

Funding

Molecular Pathogenesis Of Hereditary Spastic ParaplegiasZIANS002992 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI BLACKSTONE, CRAIG · 2009 to 2021
$20.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Hereditary spastic paraplegias are inherited neurological disorders characterized by progressive lower-limb spasticity and weakness. Although more than 50 genetic loci are known [spastic gait (SPG)1 to -57], over half of hereditary spastic paraplegia cases are caused by pathogenic mutations in four genes encoding proteins that function in tubular endoplasmic reticulum (ER) network formation: atlastin-1 (SPG3A), spastin (SPG4), reticulon 2 (SPG12), and receptor expression-enhancing protein 1 (SPG31). Here, we show that the SPG33 protein protrudin contains hydrophobic, intramembrane hairpin domains, interacts with tubular ER proteins, and functions in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Protrudin also interacts with KIF5 and harbors a Rab-binding domain, a noncanonical FYVE (Fab-1, YGL023, Vps27, and EEA1) domain, and a two phenylalanines in an acidic tract (FFAT) domain and, thus, may also function in the distribution of ER tubules via ER contacts with the plasma membrane or other organelles.

Indexed as

Adenosine TriphosphatasesEndoplasmic ReticulumGTP-Binding ProteinsHEK293 CellsHeLa CellsHumansMembrane ProteinsMembrane Transport ProteinsMutant ProteinsProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsSpastic Paraplegia, HereditarySpastinVesicular Transport ProteinsAdenosine TriphosphatasesATL1 protein, humanGTP-Binding ProteinsMembrane ProteinsMembrane Transport ProteinsMutant ProteinsRecombinant ProteinsSpastinSPAST protein, humanVesicular Transport ProteinsZFYVE27 protein, human

Identifiers

PMID23969831
PMCPMC3773775
OpenAlexW2113977012

What OpenQuestion holds

Textmetadata
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.