Evidence map›Paper›PMID 36384114›Full record

ArticleCell reports2022

Development of single-molecule ubiquitination mediated fluorescence complementation to visualize protein ubiquitination dynamics in dendrites.

Marius F Ifrim, Aleksandra Janusz-Kaminska, Gary J Bassell

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2022. 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
0.9field-weighted citation impact, top 22% 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. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  2. Article
  3. Synaptic input and CaNature neuroscience · 2024
    Article
  4. 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

3 authors at 1 institution in 1 country.

Marius F IfrimDepartment of Cell and Developmental Biology, State University of New York, Upstate Medical University, Weiskotten Hall, 766 Irving Avenue, Syracuse, NY 13210, USA; Department of Cell Biology, Emory University School of Medicine, 615 Michael St., Atlanta, GA 30322, USA. Electronic address: ifrimm@upstate.edu.
Aleksandra Janusz-KaminskaDepartment of Cell Biology, Emory University School of Medicine, 615 Michael St., Atlanta, GA 30322, USA.
Gary J BassellDepartment of Cell Biology, Emory University School of Medicine, 615 Michael St., Atlanta, GA 30322, USA. Electronic address: gbassel@emory.edu.
Emory University · US

Funding

ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2008 to 2018
$6.8M
FMRP Mechanism and FunctionR01MH109026 · NIMH · EMORY UNIVERSITY · PI BASSELL, GARY J · 2016 to 2020
$2.0M
Imaging of protein synthesis and ubiquitination in fragile x syndromeR21NS091038 · NINDS · EMORY UNIVERSITY · PI BASSELL, GARY J · 2014 to 2015
$429k
NIMH NIH HHS R01 MH109026NINDS NIH HHS P30 NS055077NINDS NIH HHS R21 NS091038
6 · The paper itself

Abstract

The ubiquitination/proteasome system is important for the spatiotemporal control of protein synthesis and degradation at synapses, while dysregulation may underlie autism spectrum disorders (ASDs). However, methods allowing direct visualization of the subcellular localization and temporal dynamics of protein ubiquitination are lacking. Here we report the development of Single-Molecule Ubiquitin Mediated Fluorescence Complementation (SM-UbFC) as a method to visualize and quantify the dynamics of protein ubiquitination in dendrites of live neurons in culture. Using SM-UbFC, we demonstrate that the rate of PSD-95 ubiquitination is elevated in dendrites of FMR1 KO neurons compared with wild-type controls. We further demonstrate the rapid ubiquitination of the fragile X messenger ribonucleoprotein, FMRP, and the AMPA receptor subunit, GluA1, which are known to be key events in the regulation of synaptic protein synthesis and plasticity. SM-UbFC will be useful for future studies on the regulation of synaptic protein homeostasis.

Indexed as

Fragile X Messenger Ribonucleoprotein 1Fragile X SyndromeDendritesFluorescenceHumansUbiquitinationFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1BiFCCP: NeuroscienceFMRPFragile X syndromeGluA1Mdm2mGluRPSD-95single-molecule imagingUbFCubiquitination

Identifiers

PMID36384114
PMCPMC9795412
OpenAlexW4309107578

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.