An Intrinsically Disordered Region in OSBP Acts as an Entropic Barrier to Control Protein Dynamics and Orientation at Membrane Contact Sites (Developmental Cell)

Oxysterol-binding protein (OSBP), which transports cholesterol at membrane contact sites (MCS), contains domains involved in membrane tethering and in lipid transfer. Jamecna et al. show that a long N-terminal intrinsically disordered sequence in OSBP limits protein density and restricts protein orientation, thereby facilitating OSBP dynamics at MCS.