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Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes

2015; American Association for the Advancement of Science; Volume: 350; Issue: 6257 Linguagem: Inglês

10.1126/science.aac7365

1095-9203

Ksenia Rostislavleva, Nicolas Soler, Yohei Ohashi, Lufei Zhang, Els Pardon, John E. Burke, Glenn R. Masson, C.M. Johnson, Jan Steyaert, Nicholas T. Ktistakis, Roger Williams,

Photosynthetic Processes and Mechanisms

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