Evidence map›Paper›PMID 23043110›Full record

ArticleThe Journal of biological chemistry2012

Phosphoinositides differentially regulate protrudin localization through the FYVE domain.

Jung-Eun Gil, Eui Kim, Il-Shin Kim, Bonsu Ku, Wei Sun Park, Byung-Ha Oh, Sung Ho Ryu, Wonhwa Cho, Won Do Heo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023
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  9. ER morphology and endo-lysosomal crosstalk: Functions and disease implications.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Roles of protrudin at interorganelle membrane contact sites.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  15. Review
  16. 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

9 authors at 3 institutions in 2 countries.

Jung-Eun GilDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea.
Eui Kim
Il-Shin Kim
Bonsu Ku
Wei Sun Park
Byung-Ha Oh
Sung Ho Ryu
Wonhwa Cho
Won Do Heo
Korea Advanced Institute of Science and Technology · KRPohang University of Science and Technology · KRUniversity of Illinois Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protrudin is a FYVE (Fab 1, YOTB, Vac 1, and EEA1) domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia. Our image-based screening of the lipid binding domain library revealed novel plasma membrane localization of the FYVE domain of protrudin unlike canonical FYVE domains that are localized to early endosomes. The membrane binding study by surface plasmon resonance analysis showed that this FYVE domain preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P(2)), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) unlike canonical FYVE domains that specifically bind phosphatidylinositol 3-phosphate (PtdIns(3)P). Furthermore, we found that these phosphoinositides (PtdInsP) differentially regulate shuttling of protrudin between endosomes and plasma membrane via its FYVE domain. Protrudin mutants with reduced PtdInsP-binding affinity failed to promote neurite outgrowth in primary cultured hippocampal neurons. These results suggest that novel PtdInsP selectivity of the protrudin-FYVE domain is critical for its cellular localization and its role in neurite outgrowth.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsCell MembraneEndosomesKineticsLipidsMiceModels, BiologicalModels, MolecularMolecular Sequence DataMutationNeuritesNIH 3T3 CellsPhosphatidylinositol PhosphatesPhosphatidylinositolsCarrier ProteinsLipidsphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsprotrudin protein, mouseVesicular Transport Proteins

Identifiers

PMID23043110
PMCPMC3510825
OpenAlexW2003577263

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.