The lipid kinase VPS34 complexes I and II are both activated by unsaturation of substrate and non-substrate lipids, curvature, electrostatics and polyphosphoinositides, which play roles in localisation and cellular function.
The conformational mechanism of a transporter protein is found to have profound and energetically costly effects on the morphology of the surrounding membrane.
Proline/glycine kink in the helical peptides affects the peptide ability to form membrane pores by stabilising toroidal pore structures but disrupting barrel-stave pore structures.
A newly discovered membrane structure associates with one of the centrioles and affects two important centrosomal events in epidermal cells – ciliary positioning and spindle orientation – through a physical interaction.
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New methods to directly visualize Rho GTPases reveal how a protein called RhoGDI regulates the activity of these 'molecular switches' at the plasma membrane.
