Animal septins contain functional transmembrane domains.

ABSTRACT: Septins are a highly conserved family of proteins that form palindromic hetero-oligomeric rods, which anneal into non-polar filaments. Via association with the plasma membrane, septin filaments recognize micron-scale membrane curvature, create diffusion barriers, and regulate cell morphogenic events via scaffolding other cytoskeletal polymers (i.e., filamentous actin [F-actin] and microtubules) and biochemical regulators of cell division, cell migration, and polarity establishment.^1,2 Although interaction with cellular membranes is thought to be crucial for septin polymer dynamics and function, how septins associate with membranes is not understood. Three polybasic regions (PB1, PB2, and PB3) and an amphipathic helix (AH) are each sufficient for membrane in

SUBMITTER: Perry JA 

PROVIDER: S-EPMC12751117 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature