ArticleScientific reports2018
Interaction of TBC1D9B with Mammalian ATG8 Homologues Regulates Autophagic Flux.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Arl8b inactivates the Rab11a recycling pathway to promote LAMP1 sorting and lysosome biogenesis.The Journal of cell biology · 2026Article
- Control of lysosome function by the GTPase-activating protein TBC1D9B and its binding partner TMEM55B.Nature communications · 2026Article
- Angiogenesis-related genes and immune microenvironment in moyamoya disease: a transcriptomic and functional analysis.Orphanet journal of rare diseases · 2025Article
- Using Machine Learning Methods to Develop Diagnostic and Prognostic mRNA Signatures for Pancreatic Cancer in Plasma Small Extracellular Vesicles.Digestive diseases and sciences · 2025Article
- A comprehensive analysis of the oncogenic and prognostic role of TBC1Ds in human hepatocellular carcinoma.PeerJ · 2024Article
- Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021Review
- Repurposing antitussive benproperine phosphate against pancreatic cancer depends on autophagy arrest.Molecular oncology · 2021Article
- Structure and Dynamics in the ATG8 Family From Experimental to Computational Techniques.Frontiers in cell and developmental biology · 2020Review
- Weighted Gene Co-Expression Network Analysis Identifies Critical Genes in the Development of Heart Failure After Acute Myocardial Infarction.Frontiers in genetics · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Autophagosomes are double-membraned vesicles with cytosolic components. Their destination is to fuse with the lysosome to degrade the enclosed cargo. However, autophagosomes may be fused with other membrane compartments and possibly misguided by the RAB molecules from these compartments. The mechanisms ensuring the proper trafficking are not well understood. Yeast ATG8 and its mammalian homologues are critically involved in the autophagosome formation and expansion. We hypothesized that they could be also involved in the regulation of autophagosome trafficking. Using the yeast two-hybrid system, we found that TBC1D9B, a GTPase activating protein for RAB11A, interacted with LC3B. TBC1D9B could also interact with other mammalian ATG8 homologues. This interaction was confirmed with purified proteins in vitro, and by co-immunoprecipitation in vivo. The interacting domain of TBC1D9B with LC3 was further determined, which is unique and different from the known LC3-interacting region previously defined in other LC3-interacting molecules. Functionally, TBC1D9B could be co-localized with LC3B on the autophagosome membranes. Inhibition of TBC1D9B suppressed the turnover of membrane-bound LC3B and the autophagic degradation of long-lived proteins. TBC1D9B can thus positively regulate autophagic flux, possibly through its GTPase activity to inactivate RAB11A, facilitating the proper destination of the autophagosomes to the degradation.
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Registered trials
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