Evidence map›Paper›PMID 39498724›Full record

ArticleBiology open2024

Intracellular dynamics of ubiquitin-like 3 visualized using an inducible fluorescent timer expression system.

Yuka Terada, Kumi Obara, Yusuke Yoshioka, Takahiro Ochiya, Haruhiko Bito, Kunihiro Tsuchida, Hiroshi Ageta, Natsumi Ageta-Ishihara

Abstract read
In one paragraph

Article in Biology open, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

8 authors.

Yuka TeradaDepartment of Biomolecular Science, Faculty of Science, Toho University, Funabashi, Chiba 274-8510, Japan.
Kumi ObaraDepartment of Biomolecular Science, Faculty of Science, Toho University, Funabashi, Chiba 274-8510, Japan.
Yusuke YoshiokaDepartment of Molecular and Cellular Medicine, Institute of Medical Science, Tokyo Medical University, Shinjyuku-ku, Tokyo 160-0023, Japan.
Takahiro OchiyaDepartment of Molecular and Cellular Medicine, Institute of Medical Science, Tokyo Medical University, Shinjyuku-ku, Tokyo 160-0023, Japan.
Haruhiko BitoDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Kunihiro TsuchidaDivision for Therapies Against Intractable Diseases, Center for Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan.ORCID 0000-0002-3983-5756
Hiroshi AgetaDivision for Therapies Against Intractable Diseases, Center for Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan.
Natsumi Ageta-IshiharaDepartment of Biomolecular Science, Faculty of Science, Toho University, Funabashi, Chiba 274-8510, Japan.ORCID 0000-0003-2543-4828

Funding

Astellas Foundation for Research on Metabolic DisordersChugai Foundation for Innovative Drug Discovery ScienceIntramural Research Grant (5-6) for Neurological and Psychiatric Disorders of the NCNPJapan Agency for Medical Research and Development 22wm0525011h0002Japan Society for the Promotion of Science JP21K07159Koyanagi-FoundationMinistry of Education, Culture, Sports, Science, and Technology, JapanPrecursory Research for Embryonic Science and Technology JPMJPR21E1Research Foundation for Opto-Science and TechnologyToho University Grant for Research Initiative ProgramToho University: Toho Daigaku
6 · The paper itself

Abstract

Exosomes are small extracellular vesicles (sEVs) secreted via multivesicular bodies (MVBs)/late endosomes and mediators of cell-cell communication. We previously reported a novel post-translational modification by ubiquitin-like 3 (UBL3). UBL3 is localized in MVBs and the plasma membrane and released outside as sEVs, including exosomes. Approximately 60% of proteins sorted in sEVs are affected by UBL3 and localized in various organelles, the plasma membrane, and the cytosol, suggesting that its dynamic movement in the cell before entering the MVBs. To examine the intracellular dynamics of UBL3, we constructed a sophisticated visualization system via fusing fluorescent timers that changed from blue to red form over time with UBL3 and by its expression under Tet-on regulation. Intriguingly, we found that after synthesis, UBL3 was initially distributed within the cytosol. Subsequently, UBL3 was localized to MVBs and the plasma membrane and finally showed predominant accumulation in MVBs. Furthermore, by super-resolution microscopy analysis, UBL3 was found to be associated with one of its substrates, α-tubulin, in the cytosol, and the complex was subsequently transported to MVBs. This spatiotemporal visualization system for UBL3 will form a basis for further studies to elucidate when and where UBL3 associates with its substrates/binding proteins before localization in MVBs.

Indexed as

UbiquitinsCell MembraneCytosolGene ExpressionHumansMultivesicular BodiesProtein TransportTubulinTubulinUbiquitinsFluorescent timersMultivesicular bodies (MVBs)Post-translational modification (PTM)Ubiquitin-like 3 (UBL3)

Identifiers

PMID39498724
PMCPMC11556312

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Registered trials

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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.