Evidence map›Paper›PMID 37250768›Full record

ArticleiScience2023

Compartmentalization of soluble endocytic proteins in synaptic vesicle clusters by phase separation.

Tomofumi Yoshida, Koh-Ichiro Takenaka, Hirokazu Sakamoto, Yusuke Kojima, Takumi Sakano, Koyo Shibayama, Koki Nakamura, Kyoko Hanawa-Suetsugu, Yasunori Mori, Yusuke Hirabayashi and 2 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

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  12. The juxtamembrane linker of synaptotagmin 1 regulates CabioRxiv : the preprint server for biology · 2023
    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

12 authors at 2 institutions in 1 country.

Tomofumi YoshidaLaboratory of Neural Membrane Biology, Graduate School of Brain Science, Doshisha University, Kyoto 610-0394, Japan.
Koh-Ichiro TakenakaLaboratory of Neural Membrane Biology, Graduate School of Brain Science, Doshisha University, Kyoto 610-0394, Japan.
Hirokazu SakamotoDepartment of Pharmacology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Yusuke KojimaDepartment of Pharmacology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Takumi SakanoDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Tokyo 113-0033, Japan.
Koyo ShibayamaDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Tokyo 113-0033, Japan.
Koki NakamuraDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Tokyo 113-0033, Japan.
Kyoko Hanawa-SuetsuguLaboratory of Neural Membrane Biology, Graduate School of Brain Science, Doshisha University, Kyoto 610-0394, Japan.
Yasunori MoriLaboratory of Neural Membrane Biology, Graduate School of Brain Science, Doshisha University, Kyoto 610-0394, Japan.
Yusuke HirabayashiDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Tokyo 113-0033, Japan.
Kenzo HiroseDepartment of Pharmacology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Shigeo TakamoriLaboratory of Neural Membrane Biology, Graduate School of Brain Science, Doshisha University, Kyoto 610-0394, Japan.
The University of Tokyo · JPDoshisha University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic vesicle (SV) clusters, which reportedly result from synapsin's capacity to undergo liquid-liquid phase separation (LLPS), constitute the structural basis for neurotransmission. Although these clusters contain various endocytic accessory proteins, how endocytic proteins accumulate in SV clusters remains unknown. Here, we report that endophilin A1 (EndoA1), the endocytic scaffold protein, undergoes LLPS under physiologically relevant concentrations at presynaptic terminals. On heterologous expression, EndoA1 facilitates the formation of synapsin condensates and accumulates in SV-like vesicle clusters via synapsin. Moreover, EndoA1 condensates recruit endocytic proteins such as dynamin 1, amphiphysin, and intersectin 1, none of which are recruited in vesicle clusters by synapsin. In cultured neurons, like synapsin, EndoA1 is compartmentalized in SV clusters through LLPS, exhibiting activity-dependent dispersion/reassembly cycles. Thus, beyond its essential function in SV endocytosis, EndoA1 serves an additional structural function by undergoing LLPS, thereby accumulating various endocytic proteins in dynamic SV clusters in concert with synapsin.

Indexed as

Biological sciencesCell biologyMolecular biology

Identifiers

PMID37250768
PMCPMC10209458
OpenAlexW4378745005

What OpenQuestion holds

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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.