Abstract
The coiled-coil domain of BECN1 serves as a protein interaction platform to recruit two major autophagy regulators ATG14 and UVRAG. Our crystal structure of the BECN1 coiled-coil domain reveals a homodimer with an imperfect dimer interface. This "imperfect" feature favors the formation of a stable BECN1-ATG14 or BECN1-UVRAG heterodimer over a metastable BECN1 homodimer to promote autophagy and/or endocytic pathways.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Vesicular Transport / metabolism*
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Animals
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Apoptosis Regulatory Proteins / chemistry*
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Apoptosis Regulatory Proteins / metabolism*
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Humans
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Models, Biological
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Protein Binding
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Protein Multimerization*
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Protein Structure, Tertiary
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Structure-Activity Relationship
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Tumor Suppressor Proteins / metabolism*
Substances
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Adaptor Proteins, Vesicular Transport
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Apoptosis Regulatory Proteins
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Tumor Suppressor Proteins