Evidence map›Paper›PMID 22352642›Full record

ArticleJournal of biomedical optics2012

Imaging protein complex formation in the autophagy pathway: analysis of the interaction of LC3 and Atg4B(C74A) in live cells using Förster resonance energy transfer and fluorescence recovery after photobleaching.

Lewis J Kraft, Anne K Kenworthy

Open access · bronzeAbstract read
In one paragraph

Article in Journal of biomedical optics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
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  11. Reduced apoptosis correlates with enhanced autophagy in synovial tissues of rheumatoid arthritis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2013
    Article
  12. 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

2 authors at 1 institution in 1 country.

Lewis J KraftVanderbilt University School of Medicine, Chemical and Physical Biology Program, Nashville, Tennessee 37232, USA.
Anne K Kenworthy
Vanderbilt University · US

Funding

Regulation of Microdomain Structure in Living CellsR01GM073846 · NIGMS · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K · 2006 to 2010
$1.3M
NIGMS NIH HHS 3R01 GM73846-4S1NIGMS NIH HHS R01 GM073846
6 · The paper itself

Abstract

The protein microtubule-associated protein 1, light chain 3 (LC3) functions in autophagosome formation and plays a central role in the autophagy pathway. Previously, we found LC3 diffuses more slowly in cells than is expected for a freely diffusing monomer, suggesting it may constitutively associate with a macromolecular complex containing other protein components of the pathway. In the current study, we used Förster resonance energy transfer (FRET) microscopy and fluorescence recovery after photobleaching (FRAP) to investigate the interactions of LC3 with Atg4B(C74A), a catalytically inactive mutant of the cysteine protease involved in lipidation and de-lipidation of LC3, as a model system to probe protein complex formation in the autophagy pathway. We show Atg4B(C74A) is in FRET proximity with LC3 in both the cytoplasm and nucleus of living cells, consistent with previous biochemical evidence that suggests these proteins directly interact. In addition, overexpressed Atg4B(C74A) diffuses significantly more slowly than predicted based on its molecular weight, and its translational diffusion coefficient is significantly slowed upon coexpression with LC3 to match that of LC3 itself. Taken together, these results suggest Atg4B(C74A) and LC3 are contained within the same multiprotein complex and that this complex exists in both the cytoplasm and nucleoplasm of living cells.

Indexed as

Fluorescence Recovery After PhotobleachingFluorescence Resonance Energy TransferAnimalsCell NucleusChlorocebus aethiopsCOS CellsCysteine EndopeptidasesCytoplasmGreen Fluorescent ProteinsMicroscopy, FluorescenceMicrotubule-Associated ProteinsModels, BiologicalMultiprotein ComplexesSingle-Cell AnalysisCysteine EndopeptidasesGreen Fluorescent ProteinsMicrotubule-Associated ProteinsMultiprotein Complexes

Identifiers

PMID22352642
PMCPMC3380812
OpenAlexW2066893348

What OpenQuestion holds

Textmetadata
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.