Evidence map›Paper›PMID 26823013›Full record

ArticleMolecular biology of the cell2016

Drosophila Nedd4-long reduces Amphiphysin levels in muscles and leads to impaired T-tubule formation.

Frozan Safi, Alina Shteiman-Kotler, Yunan Zhong, Konstantin G Iliadi, Gabrielle L Boulianne, Daniela Rotin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Regulation of SH3PX1 by dNedd4-long at theThe Journal of biological chemistry · 2019
    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

6 authors at 2 institutions in 1 country.

Frozan SafiHospital for Sick Children, Toronto, ON M5G 0A4, Canada Biochemistry Department, University of Toronto, Toronto ON M5S 1A1, Canada.
Alina Shteiman-KotlerHospital for Sick Children, Toronto, ON M5G 0A4, Canada Biochemistry Department, University of Toronto, Toronto ON M5S 1A1, Canada.
Yunan ZhongHospital for Sick Children, Toronto, ON M5G 0A4, Canada Biochemistry Department, University of Toronto, Toronto ON M5S 1A1, Canada.
Konstantin G IliadiHospital for Sick Children, Toronto, ON M5G 0A4, Canada.
Gabrielle L BoulianneHospital for Sick Children, Toronto, ON M5G 0A4, Canada Molecular Genetics Department, University of Toronto, Toronto ON M5S 1A1, Canada.
Daniela RotinHospital for Sick Children, Toronto, ON M5G 0A4, Canada Biochemistry Department, University of Toronto, Toronto ON M5S 1A1, Canada drotin@sickkids.ca.
University of Toronto · CAHospital for Sick Children · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drosophila Nedd4 (dNedd4) is a HECT ubiquitin ligase with two main splice isoforms: dNedd4-short (dNedd4S) and -long (dNedd4Lo). DNedd4Lo has a unique N-terminus containing a Pro-rich region. We previously showed that whereas dNedd4S promotes neuromuscular synaptogenesis, dNedd4Lo inhibits it and impairs larval locomotion. To delineate the cause of the impaired locomotion, we searched for binding partners to the N-terminal unique region of dNedd4Lo in larval lysates using mass spectrometry and identified Amphiphysin (dAmph). dAmph is a postsynaptic protein containing SH3-BAR domains and regulates muscle transverse tubule (T-tubule) formation in flies. We validated the interaction by coimmunoprecipitation and showed direct binding between dAmph-SH3 domain and dNedd4Lo N-terminus. Accordingly, dNedd4Lo was colocalized with dAmph postsynaptically and at muscle T-tubules. Moreover, expression of dNedd4Lo in muscle during embryonic development led to disappearance of dAmph and impaired T-tubule formation, phenocopying amph-null mutants. This effect was not seen in muscles expressing dNedd4S or a catalytically-inactive dNedd4Lo(C→A). We propose that dNedd4Lo destabilizes dAmph in muscles, leading to impaired T-tubule formation and muscle function.

Indexed as

AnimalsBinding SitesDown-RegulationDrosophila melanogasterDrosophila ProteinsLarvaMuscle DevelopmentMusclesNedd4 Ubiquitin Protein LigasesNerve Tissue ProteinsProtein IsoformsUbiquitin-Protein LigasesamphiphysinDrosophila ProteinsNedd4 protein, DrosophilaNedd4 Ubiquitin Protein LigasesNerve Tissue ProteinsProtein IsoformsUbiquitin-Protein Ligases

Identifiers

PMID26823013
PMCPMC4791135
OpenAlexW2278996712

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.