ArticleBiochemistry2016
Conformational Flexibility Enables the Function of a BECN1 Region Essential for Starvation-Mediated Autophagy.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Structural insights into Beclin 1 interactions with it's regulators for autophagy modulation.Computational and structural biotechnology journal · 2025Review
- Tumor biomarkers for diagnosis, prognosis and targeted therapy.Signal transduction and targeted therapy · 2024Review
- Invariant BECN1 CXXC motifs bind ZnAutophagy · 2024Article
- Targeting autophagy and beyond: Deconvoluting the complexity of Beclin-1 from biological function to cancer therapy.Acta pharmaceutica Sinica. B · 2023Review
- Epstein-Barr Virus Encoded BCL2, BHRF1, Downregulates Autophagy by Noncanonical Binding of BECN1.Biochemistry · 2023Article
- Review
- Differential Protein Metabolism and Regeneration in Gastrocnemius Muscles in High-fat Diet Fed Mice and Pre-hibernation Daurian Ground Squirrels: A Comparison between Pathological and Healthy Obesity.Zoological studies · 2021Article
- Autophagy-Related Beclin 1 and Head and Neck Cancers.OncoTargets and therapy · 2020Review
- Identification of Autophagy-Associated Biomarkers and Corresponding Regulatory Factors in the Progression of Colorectal Cancer.Frontiers in genetics · 2020Article
- The Role of Beclin 1-Dependent Autophagy in Cancer.Biology · 2019Review
- Beclin 1 Phosphorylation - at the Center of Autophagy Regulation.Frontiers in cell and developmental biology · 2018Review
- The Autophagy-Related Beclin-1 Protein Requires the Coiled-Coil and BARA Domains To Form a Homodimer with Submicromolar Affinity.Biochemistry · 2017Article
- Structural transitions in conserved, ordered Beclin 1 domains essential to regulating autophagy.The Journal of biological chemistry · 2017Article
- Vps34 Kinase Domain Dynamics Regulate the Autophagic PI 3-Kinase Complex.Molecular cell · 2017Article
- BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.Protein science : a publication of the Protein Society · 2017Article
- Mutation-Structure-Function Relationship Based Integrated Strategy Reveals the Potential Impact of Deleterious Missense Mutations in Autophagy Related Proteins on Hepatocellular Carcinoma (HCC): A Comprehensive Informatics Approach.International journal of molecular sciences · 2017Article
- Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions.Biochimica et biophysica acta · 2016Article
- Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond.Protein science : a publication of the Protein Society · 2016Review
- Identification of BECN1 and ATG14 Coiled-Coil Interface Residues That Are Important for Starvation-Induced Autophagy.Biochemistry · 2016Article
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9 authors.
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Abstract
BECN1 is essential for autophagy, a critical eukaryotic cellular homeostasis pathway. Here we delineate a highly conserved BECN1 domain located between previously characterized BH3 and coiled-coil domains and elucidate its structure and role in autophagy. The 2.0 Å sulfur-single-wavelength anomalous dispersion X-ray crystal structure of this domain demonstrates that its N-terminal half is unstructured while its C-terminal half is helical; hence, we name it the flexible helical domain (FHD). Circular dichroism spectroscopy, double electron-electron resonance-electron paramagnetic resonance, and small-angle X-ray scattering (SAXS) analyses confirm that the FHD is partially disordered, even in the context of adjacent BECN1 domains. Molecular dynamic simulations fitted to SAXS data indicate that the FHD transiently samples more helical conformations. FHD helicity increases in 2,2,2-trifluoroethanol, suggesting it may become more helical upon binding. Lastly, cellular studies show that conserved FHD residues are required for starvation-induced autophagy. Thus, the FHD likely undergoes a binding-associated disorder-to-helix transition, and conserved residues critical for this interaction are essential for starvation-induced autophagy.
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