Evidence map›Paper›PMID 25918845›Full record

ArticleeLife2015

Synaptojanin cooperates in vivo with endophilin through an unexpected mechanism.

Yongming Dong, Yueyang Gou, Yi Li, Yan Liu, Jihong Bai

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 44 citations in OpenAlex.

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  20. Split cGAL, an intersectional strategy using a split intein for refined spatiotemporal transgene control inProceedings of the National Academy of Sciences of the United States of America · 2018
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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

5 authors at 3 institutions in 2 countries.

Yongming DongBasic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, United States.
Yueyang GouCollege of Life Science, Sichuan University, Chengdu, China.
Yi LiCollege of Life Science, Sichuan University, Chengdu, China.
Yan LiuBasic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, United States.
Jihong BaiBasic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, United States.
Fred Hutch Cancer Center · USSichuan University · CNUniversity of Washington · US

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
Membrane Bending Machinery for Synaptic Vesicle EndocytosisR01NS085214 · NINDS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BAI, JIHONG · 2013 to 2017
$1.9M
Mechanisms of Synapse RemodelingR00MH085039 · NIMH · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BAI, JIHONG · 2011 to 2013
$727k
NIH HHS P40 OD010440NIMH NIH HHS R00-MH085039NINDS NIH HHS R01 NS085214NINDS NIH HHS R01-NS085214
6 · The paper itself

Abstract

Synaptojanin and endophilin represent a classic pair of endocytic proteins that exhibit coordinated action during rapid synaptic vesicle endocytosis. Current models suggest that synaptojanin activity is tightly associated with endophilin through high-affinity binding between the synaptojanin proline-rich domain (PRD) and the endophilin SH3 domain. Surprisingly, we find that truncated synaptojanin lacking the PRD domain sustains normal synaptic transmission, indicating that synaptojanin's core function in vivo resides in the remaining two domains that contain phosphoinositide-phosphatase activities: an N-terminal Sac1 phosphatase domain and a 5-phosphatase domain. We further show that the Sac1 domain plays an unexpected role in targeting synaptojanin to synapses. The requirement for Sac1 is bypassed by tethering the synaptojanin 5-phophatase to the endophilin membrane-bending Bin-Amphiphysin-Rvs (BAR) domain. Together, our results uncover an unexpected role for the Sac1 domain in vivo in supporting coincident action between synaptojanin and endophilin at synapses.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansDNA-Binding ProteinsEndocytosisGene Transfer TechniquesMicroinjectionsNerve Tissue ProteinsPhosphoric Monoester HydrolasesSynapsesSynaptic TransmissionTransposasesAdaptor Proteins, Signal TransducingDNA-Binding Proteinsmariner transposasesNerve Tissue ProteinsPhosphoric Monoester HydrolasessynaptojaninTransposasesC. eleganscell biologyendocytosisendophilinneuroscienceSac1 phosphatase domainsynaptic transmissionsynaptojanin

Identifiers

PMID25918845
PMCPMC4435004
OpenAlexW1999290808

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.