title: Time to Fold: Tom1 Uses New Tricks to Regulate Lipid Binding of Tollip.
abstract: In this issue of Structure, Xiao et al. (2015) describe a new mechanism of regulation of lipid binding. Structural and functional studies demonstrate that Tom1 interactions with the cargo sorting protein Tollip induce the partially unfolded Tom1-binding domain of Tollip to fold. This folding modulates lipid binding of Tollip, mediating its dissociation from PI(3)P and committing Tollip to cargo trafficking.
authors.affiliation: Department of Biochemistry & Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, IN 46617, USA; Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. Electronic address: rstaheli@iu.edu.
authors.forename: Robert V
authors.initials: RV
authors.lastname: Stahelin
mesh_terms: D011992:Endosomes / Q000737:chemistry*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D018129:Phosphatidylinositol Phosphates / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D018129:Phosphatidylinositol Phosphates; D011506:Proteins; D011993:Recombinant Fusion Proteins; D025801:Ubiquitin