Dehydrins are intrinsically disordered proteins known for their ability to confer desiccation tolerance to plants, potentially through the protection of DNA, membranes, and proteins. With the Vitis riparia dehydrin VrDHN1, I explore potential mechanisms for nuclear localization through phosphorylation of the S-segment and/or the proposed nuclear localization signal called the basic domain. Using pseudophosphorylated constructs, I show that the nuclear to cytoplasmic ratio did not increase proportionally to the level of pseudophosphorylation in the S-segment, but that the S70E mutation caused a 27% increase in nuclear localization. Blocking phosphorylation and basic domain binding did not prevent nuclear localization, suggesting that phosphorylation may result in a shift from passive to active transport. In membrane binding and protein cryoprotection assays, pseudophosphorylation resulted in increased α-helicity in the presence of SDS, and a reduced PD50 in the LDH assay, indicative of improved cryoprotective efficiency. Further work investigating the potential phosphorylation-mediated active-to-passive switch is required.