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

DOI: 10.1126/science.aac7365 DOI Help

Authors: K. Rostislavleva (MRC Laboratory of Molecular Biology) , N. Soler (MRC Laboratory of Molecular Biology) , Y. Ohashi (MRC Laboratory of Molecular Biology) , L. Zhang (MRC Laboratory of Molecular Biology) , E. Pardon (Structural Biology Research Center, VIB) , J. Burke (MRC Laboratory of Molecular Biology, U.K.) , G. Masson (MRC Laboratory of Molecular Biology, U.K.) , C. Johnson (MRC Laboratory of Molecular Biology) , J. Steyaert (Structural Biology Research Center, VIB) , N. T. Ktistakis (The Babraham Institute) , R. L. Williams (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science , VOL 350 , PAGES aac7365 - aac7365

State: Published (Approved)
Published: October 2015
Diamond Proposal Number(s): 11235

Open Access Open Access

Abstract: 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.

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I23-Long wavelength MX

Other Facilities: ESRF ID29