Ca ²⁺ Regulates Dimerization of the BAR Domain Protein PICK1 and Consequent Membrane Curvature.

ABSTRACT: Bin-Amphiphysin-Rvs (BAR) domain proteins are critical regulators of membrane geometry. They induce and stabilize membrane curvature for processes, such as clathrin-coated pit formation and endosomal membrane tubulation. BAR domains form their characteristic crescent-shaped structure in the dimeric form, indicating that the formation of the dimer is critical to their function of inducing membrane curvature and suggesting that a dynamic monomer-dimer equilibrium regulated by cellular signaling would be a powerful mechanism for controlling BAR domain protein function. However, to the best of our knowledge, cellular mechanisms for regulating BAR domain dimerization remain unexplored. PICK1 is a Ca²⁺-binding BAR domain protein involved in the endocytosis and endosomal recycling of n

SUBMITTER: Stan GF 

PROVIDER: S-EPMC9201945 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature