Impact of N-terminal dimerization on formin homology 1 domain polymer dynamics and actin assembly.

ABSTRACT: Many proteins contain intrinsically disordered regions (IDRs) that lack stable 3-dimensional structure. IDR behavior is poorly understood, leading to challenges for biochemical and computational analysis of IDR-containing proteins. Formins are a diverse set of homodimers containing an IDR - the FH1 domain - that facilitates polymerization of the cytoskeletal protein actin by increasing the local concentration of actin monomers at the actin assembly site. A commonly accepted model of formin-based actin polymerization involves a capture-and-deliver process: one or more binding sites (proline-rich motifs, PRMs) "capture" actin monomers and then "deliver" actin to the actin assembly site. There is evidence that formin FH1 domains are dimerized on both ends, but much research has been performed

SUBMITTER: Bogue K 

PROVIDER: S-EPMC12667827 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature