Dynamic structure of the full-length scaffolding protein NHERF1 influences signaling complex assembly.

ABSTRACT: The Na⁺/H⁺ exchange regulatory cofactor 1 (NHERF1) protein modulates the assembly and intracellular trafficking of several transmembrane G protein-coupled receptors (GPCRs) and ion transport proteins with the membrane-cytoskeleton adapter protein ezrin. Here, we applied solution NMR and small-angle neutron scattering (SANS) to structurally characterize full-length NHERF1 and disease-associated variants that are implicated in impaired phosphate homeostasis. Using NMR, we mapped the modular architecture of NHERF1, which is composed of two structurally-independent PDZ domains that are connected by a flexible, disordered linker. We observed that the ultra-long and disordered C-terminal tail of NHERF1 has a type 1 PDZ-binding motif that interacts weakly with the proximal,

SUBMITTER: Bhattacharya S 

PROVIDER: S-EPMC6643037 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature