Lipid scrambling assay and yeast growth assay data demonstrating the ability of IST2 to (i) scramble lipids in vitro and (ii) facilitate lipid transport by Osh6 in S.cerevisiae

In the associated article, we present a comprehensive investigation
elucidating structural and mechanistic properties of the tethering protein
IST2 and its interaction with the soluble lipid transport protein OSH6.
The ER-embedded transmembrane domain of IST2 is homologous to the TMEM16
family and acts as constitutively active lipid scramblase. The extended
C-terminus binds to the plasma membrane and the PS/PI4P exchanger OSH6.
Through cellular growth assays, biochemical and structural studies, we
have elucidated the interaction between both proteins and provide evidence
that OSH6 remains associated with IST2 during lipid shuttling between
membranes. The dataset features raw data from lipid scrambling and
cellular yeast complementation assays.