ArticleAutophagy2021
RAB33B recruits the ATG16L1 complex to the phagophore via a noncanonical RAB binding protein.
Article in Autophagy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 35 citations in OpenAlex.
- From lipid modification to cell death: the diverse roles of S-palmitoylation in cell fate decisions.Cell communication and signaling : CCS · 2026Review
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- A comprehensive analysis of the relationship between inflammasomes and autophagy in human tumors: Recent developments.Journal of cell communication and signaling · 2025Review
- Two specific interactions of GATE16 with TRPML3 and RAB33B regulate autophagy.Scientific reports · 2025Article
- The Parkinson Disease-Associated Mutant DNAJC13(N855S) Leads to Its Accelerated Degradation and Negatively Affects Macroautophagy and Retromer Complex-Mediated Dynamics.Journal of cellular physiology · 2025Article
- Host cellular protein RAB33B facilitates influenza viral replication and modulates M2 trafficking by enhancing autophagy.Veterinary research · 2025Article
- Targeting secretory autophagy in solid cancers: mechanisms, immune regulation and clinical insights.Experimental hematology & oncology · 2025Review
- Hepatitis B virus entry, assembly, and egress.Microbiology and molecular biology reviews : MMBR · 2024Review
- ZDHHC7-mediatedAutophagy · 2024Article
- When an underdog becomes a major player: the role of protein structural disorder in the Atg8 conjugation system.Autophagy · 2024Review
- Review
- Three-step docking by WIPI2, ATG16L1, and ATG3 delivers LC3 to the phagophore.Science advances · 2024Article
- Osteogenic mechanism of chlorogenic acid and its application in clinical practice.Frontiers in pharmacology · 2024Review
- Coiled-coil-mediated dimerization of Atg16 is required for binding to the PROPPIN Atg21.Open biology · 2023Article
- Rab41-mediated ESCRT machinery repairs membrane rupture by a bacterial toxin in xenophagy.Nature communications · 2023Article
- An ATG12-ATG5-TECPR1 E3-like complex regulates unconventional LC3 lipidation at damaged lysosomes.EMBO reports · 2023Article
- Article
- ATG16L1 adopts a dual-binding site mode to interact with WIPI2b in autophagy.Science advances · 2023Article
- Structural biology of the Atg8 and Atg12 conjugation systems.Autophagy reports · 2023Review
- The role of ATG16L2 in autophagy and disease.Autophagy · 2022Review
Corrections and comments
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Authors and funding
7 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autophagosome formation is a fundamental process in macroautophagy/autophagy, a conserved self-eating mechanism in all eukaryotes, which requires the conjugating ATG (autophagy related) protein complex, ATG12-ATG5-ATG16L1 and lipidated MAP1LC3/LC3 (microtubule associated protein 1 light chain 3). How the ATG12-ATG5-ATG16L1 complex is recruited to membranes is not fully understood. Here, we demonstrated that RAB33B plays a key role in recruiting the ATG16L1 complex to phagophores during starvation-induced autophagy. Crystal structures of RAB33B bound to the coiled-coil domain (CCD) of ATG16L1 revealed the recognition mechanism between RAB33B and ATG16L1. ATG16L1 is a novel RAB-binding protein (RBP) that can induce RAB proteins to adopt active conformation without nucleotide exchange. RAB33B and ATG16L1 mutually determined the localization of each other on phagophores. RAB33B-ATG16L1 interaction was required for LC3 lipidation and autophagosome formation. Upon starvation, a fraction of RAB33B translocated from the Golgi to phagophores and recruited the ATG16L1 complex. In this work, we reported a new mechanism for the recruitment of the ATG12-ATG5-ATG16L1 complex to phagophores by RAB33B, which is required for autophagosome formation.
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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.