ORP2 is a sterol-binding protein with documented functions in lipid and glucose metabolism,
Akt signaling, steroidogenesis, cell adhesion, migration and proliferation. Here we
investigate the interactions of ORP2 with phosphoinositides (PIPs) by surface plasmon
resonance (SPR), its affinity for cholesterol with a pull-down assay, and its capacity to
transfer sterol in vitro. Moreover, we determine the effects of wild-type (wt) ORP2 and a
mutant with attenuated PIP binding, ORP2 (mHHK), on the subcellular distribution of …