ArticleAutophagy2016
The BECN1 N-terminal domain is intrinsically disordered.
Article in Autophagy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Comprehensive analysis of regulated cell death pathways: intrinsic disorder, protein-protein interactions, and cross-pathway communication.Apoptosis : an international journal on programmed cell death · 2025Pooled it
- Impact of BECLIN1 haploinsufficiency on goblet cell function and susceptibility to colitis.Cell death & disease · 2026Article
- Review
- The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025Review
- BECLIN-1/BECN1 at the barrier: a gatekeeper of epithelial and endothelial homeostasis.Autophagy reports · 2025Review
- Structural insights into Beclin 1 interactions with it's regulators for autophagy modulation.Computational and structural biotechnology journal · 2025Review
- Invariant BECN1 CXXC motifs bind ZnAutophagy · 2024Article
- Review
- Isolation, Characterization, and Autophagy Function of BECN1-Splicing Isoforms in Cancer Cells.Biomolecules · 2022Article
- Review
- The Bcl-2 Family: Ancient Origins, Conserved Structures, and Divergent Mechanisms.Biomolecules · 2020Review
- Autophagy-Related Beclin 1 and Head and Neck Cancers.OncoTargets and therapy · 2020Review
- The Role of Beclin 1-Dependent Autophagy in Cancer.Biology · 2019Review
- Structural insights into BCL2 pro-survival protein interactions with the key autophagy regulator BECN1 following phosphorylation by STK4/MST1.Autophagy · 2019Article
- Post-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation.Cell death and differentiation · 2019Review
- 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
- BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.Protein science : a publication of the Protein Society · 2017Article
- Phosphoglycerate Kinase 1 Phosphorylates Beclin1 to Induce Autophagy.Molecular cell · 2017Article
- Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond.Protein science : a publication of the Protein Society · 2016Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BECN1/Beclin 1 has a critical role in the early stages of autophagosome formation. Recently, structures of its central and C-terminal domains were reported, however, little structural information is available on the N-terminal domain, comprising a third of the protein. This lack of structural information largely stems from the inability to produce this region in a purified form. Here, we describe the expression and purification of the N-terminal domain of BECN1 (residues 1 to 150) and detailed biophysical characterization, including NMR spectroscopy. Combined, our studies demonstrated at the atomic level that the BECN1 N-terminal domain is intrinsically disordered, and apart from the BH3 subdomain, remains disordered following interaction with a binding partner, BCL2L1/BCL-XL. In addition, the BH3 domain α-helix induced upon interaction with BCL2L1 reverts to a disordered state when the complex is dissociated by exposure to a competitive inhibitor. No significant interactions between N- and C-terminal domains were detected.
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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.