The ubiquitin ligase Nedd4-2 promotes localization of DNMBP/Tuba to P-bodies under hyperosmotic stress.

Zetao Liu, Chong Jiang, Faith Yeung, Brian Raught, Daniela Rotin

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2025. 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.

Identification of E3 ligase substrates and PROTAC-induced ubiquitylation sites using proximity-based identification of ubiquitin sites (PrIUS).Communications biology · 2026
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

5 authors.

Zetao LiuCell & Systems Biology Program, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.

Chong JiangCell & Systems Biology Program, The Hospital for Sick Children, Toronto, Ontario, Canada.

Faith YeungPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada; Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.

Brian RaughtPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada; Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.

Daniela RotinCell & Systems Biology Program, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. Electronic address: drotin@sickkids.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin ligase Nedd4-2/NEDD4L, comprised of C2-WW(x4)-HECT domains, is known to regulate several ion transporters and channels. We recently showed that elevated intracellular [Na

Indexed as

Carrier ProteinsEndosomal Sorting Complexes Required for TransportNedd4 Ubiquitin Protein LigasesOsmotic PressureUbiquitin-Protein LigasesAnimalscdc42 GTP-Binding ProteinHEK293 CellsHeLa CellsHumansMembrane Proteinsp38 Mitogen-Activated Protein KinasesCarrier Proteinscdc42 GTP-Binding ProteinCDC42 protein, humanEndosomal Sorting Complexes Required for TransportMembrane ProteinsNDFIP1 protein, humanNedd4L protein, humanNedd4 protein, humanNedd4 Ubiquitin Protein Ligasesp38 Mitogen-Activated Protein KinasesUbiquitin-Protein Ligasescondensatesdynamin-binding proteinNEDD4Losmolarity

Identifiers

PMID40975170

DOI10.1016/j.jbc.2025.110738

PMCPMC12569825

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.