
Opening up Vps34 protein complexes During intracellular membrane trafficking, large protein complexes regulate and adapt the activity of signal transducer enzymes such as the class III phosphatidylinositol 3-kinase Vps34. These large enzyme complexes are present in all eukaryotic cells, having widespread importance in neurodegeneration, aging, and cancer; however, a structural understanding has been lacking. Rostislavleva et al. provide atomic-resolution insights into the structures of the Vps34-containing protein complexes required for autophagy, endocytic sorting, and cytokinesis. The V-shaped complexes can undergo opening motions, which allows them to adapt to and phosphorylate membranes. Science , this issue p. 10.1126/science.aac7365
570, Cell Membrane, 610, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Class III Phosphatidylinositol 3-Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Vacuolar Sorting Protein VPS15, name=General, /dk/atira/pure/subjectarea/asjc/1000, Protein Multimerization
570, Cell Membrane, 610, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Class III Phosphatidylinositol 3-Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Vacuolar Sorting Protein VPS15, name=General, /dk/atira/pure/subjectarea/asjc/1000, Protein Multimerization
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