ArticleAutophagy2019
GAN (gigaxonin) E3 ligase and ATG16L1: master and commander of autophagosome production.
Article in Autophagy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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.
Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Disease mutation in gigaxonin-E3 ligase recapitulates giant axonal neuropathy in mice.Acta neuropathologica communications · 2025Article
- A multilevel screening pipeline in zebrafish identifies therapeutic drugs for GAN.EMBO molecular medicine · 2023Article
- Neurofilaments in health and Charcot-Marie-Tooth disease.Frontiers in cell and developmental biology · 2023Review
- Autophagy and Its Association with Genetic Mutations in Parkinson Disease.Medical science monitor : international medical journal of experimental and clinical research · 2022Review
- E3 Ubiquitin Ligases in Neurological Diseases: Focus on Gigaxonin and Autophagy.Frontiers in physiology · 2020Review
Corrections and comments
- Comment on
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sequential action of ATG proteins guarantees the formation of the autophagosome from the steps of the induction, nucleation, elongation and sealing of the phagophore membrane. Posttranslational modifications further add to the fine-tuning regulation of this highly ordered machinery and confer, in space and time, the dynamics necessary to respond to macroautophagy/autophagy activation, and to shut it down. Recently, we reported the discovery of GAN (gigaxonin), an E3 ubiquitin ligase adaptor as a key regulator of the elongation step of phagophore formation. GAN interacts, ubiquitinates and degrades ATG16L1, which forms a complex with the ATG12-ATG5 ubiquitin-like conjugation system, and specifies the site of lipidation of LC3 by this complex onto the nascent phagophore. Accordingly, depletion of GAN in primary neurons causes the accumulation of ATG16L1 and decreases the autophagy flux by impairing the net production of autophagosomes. Considering the pivotal role of ATG16L1 in autophagy, and the reversal of the deficits upon reintroduction of GAN, one can speculate that GAN constitutes a novel molecular switch to fine tune the autophagy machinery.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.