Title: Intrinsically Disordered Region of Actin Binding Protein Regulates Dynamic Actin Assembly
Abstract: Assembly of the actin cytoskeleton are dynamically regulated under various physiological and pathological states to fine-tune the endocytosis, cytokinesis and vesicular transport. A particularly interesting phenomenon is that both endocytic proteins and ABPs are highly enriched of intrinsically disordered regions (IDRs), which were recently found as a constituent of protein crowding, protein coacervation, and phase separation. How the actin filament assembly are regulated by these intrinsically disordered regions are largely unclear, which are important for understudying in vivo complex regulation of actin polymerization and organization. The protein dynamics, conformation, inter- or intramolecular interactions for intrinsically disordered proteins (IDPs) are highly regulated by the changes of surface electrostatic interactions through the post-translational modifications, such as protein phosphorylation. We recently studied several ABPs and found striking regulation of actin filament assembly through the IDR and the phospho-regulation of IDR of actin binding proteins. We will present and discuss the molecular mechanisms by which actin assembly receives multi-signals from intracellular or extracellular cues in modulating actin filament assembly.