Structure of the Human Atg13-Atg101 HORMA Heterodimer: an Interaction Hub within the ULK1 Complex
Copyright policy )Structure of the Human Atg13-Atg101 HORMA Heterodimer: an Interaction Hub within the ULK1 Complex
The ULK1 complex, consisting of the ULK1 protein kinase itself, FIP200, Atg13, and Atg101, controls the initiation of autophagy in animals. We determined the structure of the complex of the human Atg13 HORMA (Hop1, Rev7, Mad2) domain in complex with the full-length HORMA domain-only protein Atg101. The two HORMA domains assemble with an architecture conserved in the Mad2 conformational heterodimer and the S. pombe Atg13-Atg101 HORMA complex. The WF finger motif that is essential for function in human Atg101 is sequestered in a hydrophobic pocket, suggesting that the exposure of this motif is regulated. Benzamidine molecules from the crystallization solution mark two hydrophobic pockets that are conserved in, and unique to, animals, and are suggestive of sites that could interact with other proteins. These features suggest that the activity of the animal Atg13-Atg101 subcomplex is regulated and that it is an interaction hub for multiple partners.
- University of California, San Francisco United States
- Lawrence Berkeley National Laboratory United States
- QB3 United States
- University of California, Santa Cruz United States
- University of California, Berkeley United States
Models, Molecular, autophagy, Molecular Sequence Data, Autophagy-Related Proteins, Gene Expression, Protein Serine-Threonine Kinases, Crystallography, X-Ray, Structural Biology, Autophagy, Animals, Autophagy-Related Protein-1 Homolog, Humans, Amino Acid Sequence, protein structure, Molecular Biology, X-ray crystallography, Adaptor Proteins, Signal Transducing, Binding Sites, Intracellular Signaling Peptides and Proteins, hydrogen-deuterium exchange, Benzamidines, Mad2 Proteins, Mutation, Atg1, Protein Multimerization, Hydrophobic and Hydrophilic Interactions, Protein Binding
Models, Molecular, autophagy, Molecular Sequence Data, Autophagy-Related Proteins, Gene Expression, Protein Serine-Threonine Kinases, Crystallography, X-Ray, Structural Biology, Autophagy, Animals, Autophagy-Related Protein-1 Homolog, Humans, Amino Acid Sequence, protein structure, Molecular Biology, X-ray crystallography, Adaptor Proteins, Signal Transducing, Binding Sites, Intracellular Signaling Peptides and Proteins, hydrogen-deuterium exchange, Benzamidines, Mad2 Proteins, Mutation, Atg1, Protein Multimerization, Hydrophobic and Hydrophilic Interactions, Protein Binding
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