Evidence map›Paper›PMID 40631620›Full record

ArticleJournal of biochemistry2025

UNC5B is an isoform-dependent target for ectodomain shedding.

Kotaro Sugimoto, Eichi Watabe, Mio Takuma, Kaname Nagahara, Toshinori Sawano, Mihoko Kajita, Junichi Takagi, Hidehito Kuroyanagi, Kyoko Shirakabe

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Kotaro SugimotoDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.
Eichi WatabeMedical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan.
Mio TakumaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.
Kaname NagaharaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.
Toshinori SawanoDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.
Mihoko KajitaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.
Junichi TakagiInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Hidehito KuroyanagiMedical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan.
Kyoko ShirakabeDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan.ORCID 0000-0002-1563-1134

Funding

Astellas Foundation for Research on Metabolic DisordersJSPS KAKENHI JP18K06911Naito FoundationTakeda Science Foundation
6 · The paper itself

Abstract

Ectodomain shedding (shedding) is a processing mechanism that cleaves the juxtamembrane region of membrane proteins and solubilizes almost the entire extracellular domain. Shedding irreversibly regulates the localization and function of membrane proteins; however, its physiological role is not fully understood. Previously, we showed that the shedding susceptibility of multiple membrane proteins is altered by skipping or inclusion of skipping exon(s) that encode their juxtamembrane region. In this study, we screened the skipping exon encoding the juxtamembrane region of membrane proteins and found that the shedding susceptibility of UNC5B, a Netrin-1 receptor, is altered by skipping or inclusion of the skipping exon encoding its juxtamembrane region. These results raise the possibility that the biological phenomena involving UNC5B, including neural circuit formation, angiogenesis and cancer development, are regulated by shedding in a splice isoform-dependent manner.

Indexed as

Netrin ReceptorsProtein DomainsAnimalsExonsHEK293 CellsHumansProtein IsoformsNetrin ReceptorsProtein IsoformsUNC5B protein, humanalternative splicingectodomain sheddingskipping exontransmembrane domainUNC5B

Identifiers

PMID40631620
PMCPMC12480741

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.