A disordered tether to iLID improves photoswitchable protein patterning on model membranes.
Daniele Di IorioJohanna BergmannSayuri L HigashiArne HoffmannSeraphine Valeska WegnerPublished in: Chemical communications (Cambridge, England) (2023)
Reversible protein patterning on model membranes is important to reproduce spatiotemporal protein dynamics in vitro . An engineered version of iLID, disiLID, with a disordered domain as a membrane tether improves the recruitment of Nano under blue light and the reversibility in the dark, which enables protein patterning on membranes with higher spatiotemporal precision.