ArticleProtein science : a publication of the Protein Society2017
BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- The emerging role of autophagy in the rewarding and stimulant behaviors in models of substance use disorder.Frontiers in neuroscience · 2026Review
- The Biological Role and Clinical Significance of BECLIN-1 in Cancer.International journal of molecular sciences · 2025Review
- The potent BECN2-ATG14 coiled-coil interaction is selectively critical for endolysosomal degradation of GPRASP1/GASP1-associated GPCRs.Autophagy · 2023Article
- Article
- The metastable states of proteins.Protein science : a publication of the Protein Society · 2020Review
- Targeting the potent Beclin 1-UVRAG coiled-coil interaction with designed peptides enhances autophagy and endolysosomal trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Protein Science best paper awards to Minfei Su and Chang-Ting Lin.Protein science : a publication of the Protein Society · 2018Article
- Structural transitions in conserved, ordered Beclin 1 domains essential to regulating autophagy.The Journal of biological chemistry · 2017Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
ATG14 binding to BECN/Beclin homologs is essential for autophagy, a critical catabolic homeostasis pathway. Here, we show that the α-helical, coiled-coil domain (CCD) of BECN2, a recently identified mammalian BECN1 paralog, forms an antiparallel, curved homodimer with seven pairs of nonideal packing interactions, while the BECN2 CCD and ATG14 CCD form a parallel, curved heterodimer stabilized by multiple, conserved polar interactions. Compared to BECN1, the BECN2 CCD forms a weaker homodimer, but binds more tightly to the ATG14 CCD. Mutation of nonideal BECN2 interface residues to more ideal pairs improves homodimer self-association and thermal stability. Unlike BECN1, all BECN2 CCD mutants bind ATG14, although more weakly than wild type. Thus, polar BECN2 CCD interface residues result in a metastable homodimer, facilitating dissociation, but enable better interactions with polar ATG14 residues stabilizing the BECN2:ATG14 heterodimer. These structure-based mechanistic differences in BECN1 and BECN2 homodimerization and heterodimerization likely dictate competitive ATG14 recruitment.
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Registered trials
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