Septins belong to a family of proteins that is highly conserved in eukaryotes and is
increasingly recognized as a novel component of the cytoskeleton. All septins are GTP …

GTP-binding (G) proteins constitute a class of P-loop (phosphate-binding loop) proteins that
work as molecular switches between the GDP-bound OFF and the GTP-bound ON state. The …

In order to fully understand any complex biochemical system from a mechanistic point of
view, it is necessary to have access to the three-dimensional structures of the molecular …

Septins are a conserved family of GTP-binding proteins that assemble into symmetric linear
heterooligomeric complexes, which in turn are able to polymerize into apolar filaments and …

Septins comprise a conserved family of proteins that are found primarily in fungi and
animals. These GTP-binding proteins have several roles during cell division, cytoskeletal …

Mitotic yeast cells express five septins (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1/Sep7). Only
Shs1 is nonessential. The four essential septins form a complex containing two copies of …

Cell shape is well described by membrane curvature. Septins are filament-forming, GTP-
binding proteins that assemble on positive, micrometer-scale curvatures. Here, we examine …

Septins are conserved GTP-binding proteins that assemble into hetero-oligomeric
complexes and higher-order structures such as filaments, rings, hourglasses or gauzes …

Septins assemble into filaments and higher-order structures that act as scaffolds for diverse
cell functions including cytokinesis, cell polarity, and membrane remodeling. Despite their …

Septins are GTP-binding proteins that form filaments and higher-order structures on the cell
cortex of eukaryotic cells and associate with actin and microtubule cytoskeletal networks …