Septins are GTP binding proteins considered to be novel components of the cytoskeleton.
They polymerize into filaments based on hexameric or octameric core particles in which two …

Mammalian septins comprise a family of 13 genes that encode GTP-binding proteins.
Specific combinations of septins can hetero-oligomerize and form filaments in vivo and in …

Septins form a conserved family of filament forming GTP binding proteins found in a wide
range of eukaryotic cells. They share a common structural architecture consisting of an N …

Septins are conserved GTP-binding cytoskeletal proteins that polymerize into filaments by
end-to-end joining of hetero-oligomeric complexes. In human cells, both hexamers and …

The septins are filament‐forming proteins found in diverse eukaryotes from fungi to
vertebrates, with roles in cytokinesis, shaping of membranes and modifying cytoskeletal …

Septins are members of a conserved family of cytoskeletal GTPases present in organisms as
diverse as yeast and mammals. Unlike lower eukaryotic cells, the physiological significance …

Septins are GTP-binding and membrane-interacting proteins with a highly conserved
domain structure involved in various cellular processes, including cytoskeleton organization …

Septin GTP-binding proteins contribute essential biological functions that range from the
establishment of cell polarity to animal tissue morphogenesis. Human septins in cells form …

Septins are conserved GTP-binding proteins that assemble into lateral diffusion barriers and
molecular scaffolds. Vertebrate genomes contain 9–17 septin genes that encode both …

Septins are able to polymerize into long apolar filaments and have long been considered to
be a component of the cytoskeleton alongside intermediate filaments (which are also apolar …