A complete compendium of crystal structures for the human SEPT3 subgroup reveals functional plasticity at a specific septin interface.

ABSTRACT: Human septins 3, 9 and 12 are the only members of a specific subgroup of septins that display several unusual features, including the absence of a C-terminal coiled coil. This particular subgroup (the SEPT3 septins) are present in rod-like octameric protofilaments but are lacking in similar hexameric assemblies, which only contain representatives of the three remaining subgroups. Both hexamers and octamers can self-assemble into mixed filaments by end-to-end association, implying that the SEPT3 septins may facilitate polymerization but not necessarily function. These filaments frequently associate into higher order complexes which associate with biological membranes, triggering a wide range of cellular events. In the present work, a complete compendium of crystal structures for the GTP-bin

SUBMITTER: Castro DKSDV 

PROVIDER: S-EPMC7201284 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature