Evidence map›Paper›PMID 23482084›Full record

ArticleAutophagy2013

LC3 fluorescent puncta in autophagosomes or in protein aggregates can be distinguished by FRAP analysis in living cells.

Liang Wang, Min Chen, Jie Yang, Zhihong Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  5. Autophagy-Mediated Suppression of Tumor Growth by Food-Grade Lipid Nanoparticles in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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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

4 authors at 3 institutions in 2 countries.

Liang WangBritton Chance Center for Biomedical Photonics; Wuhan National Laboratory for Optoelectronics-Huazhong University of Science and Technology, Wuhan, China.
Min Chen
Jie Yang
Zhihong Zhang
Huazhong University of Science and Technology · CNHuazhong University of Science and Technology Hospital · CNPhotonics (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LC3 is a marker protein that is involved in the formation of autophagosomes and autolysosomes, which are usually characterized and monitored by fluorescence microscopy using fluorescent protein-tagged LC3 probes (FP-LC3). FP-LC3 and even endogenous LC3 can also be incorporated into intracellular protein aggregates in an autophagy-independent manner. However, the dynamic process of LC3 associated with autophagosomes and autolysosomes or protein aggregates in living cells remains unclear. Here, we explored the dynamic properties of the two types of FP-LC3-containing puncta using fluorescence microscopy techniques, including fluorescence recovery after photobleaching (FRAP) and fluorescence resonance energy transfer (FRET). The FRAP data revealed that the fluorescent signals of FP-LC3 attached to phagophores or in mature autolysosomes showed either minimal or no recovery after photobleaching, indicating that the dissociation of LC3 from the autophagosome membranes may be very slow. In contrast, FP-LC3 in the protein aggregates exhibited nearly complete recovery (more than 80%) and rapid kinetics of association and dissociation (half-time < 1 sec), indicating a rapid exchange occurs between the aggregates and cytoplasmic pool, which is mainly due to the transient interaction of LC3 and SQSTM1/p62. Based on the distinct dynamic properties of FP-LC3 in the two types of punctate structures, we provide a convenient and useful FRAP approach to distinguish autophagosomes from LC3-involved protein aggregates in living cells. Using this approach, we find the FP-LC3 puncta that adjacently localized to the phagophore marker ATG16L1 were protein aggregate-associated LC3 puncta, which exhibited different kinetics compared with that of autophagic structures.

Indexed as

AutophagyAdaptor Proteins, Signal TransducingAnimalsAutophagy-Related ProteinsCarrier ProteinsCell SurvivalFluorescence Recovery After PhotobleachingFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHeLa CellsHumansLysosomesMiceMicrotubule-Associated ProteinsPhagosomesProtein BindingAdaptor Proteins, Signal TransducingATG16L1 protein, humanAutophagy-Related ProteinsCarrier ProteinsGreen Fluorescent ProteinsMicrotubule-Associated ProteinsRecombinant Fusion ProteinsSequestosome-1 ProteinSQSTM1 protein, humanautophagosomeFRAPFRETinclusion bodyLC3protein aggregate

Identifiers

PMID23482084
PMCPMC3669184
OpenAlexW2009069894

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.