The actin and microtubule cytoskeletons comprise a variety of networks with distinct
architectures, dynamics and protein composition. A fundamental question in eukaryotic cell …

Septins are conserved GTP-binding proteins that associate with cellular membranes and the
actin and microtubule cytoskeletons. They polymerize to form filamentous structures that act …

Septins are an integral component of the cytoskeleton, assembling into higher-order
oligomers and filamentous polymers that associate with actin filaments, microtubules and …

Cellular morphogenesis and processes such as cell division and migration require the
coordination of the microtubule and actin cytoskeletons. Microtubule–actin crosstalk is …

Septins are conserved guanine nucleotide-binding proteins that polymerize into filaments at
the cell cortex or in association with other cytoskeletal proteins, such as actin or …

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 …

Septins are a family of conserved proteins that have been implicated in a variety of cellular
functions involving specialized regions of the cell cortex and changes in cell shape. The …

Septins are ubiquitous GTP-binding proteins generally regarded as cytoskeletal
components. Higher-order septin assemblies represented by the yeast septin collar function …

Septins comprise an evolutionarily conserved family of oligomeric GTPases that regulate the
intracellular localization of proteins by functioning as protein scaffolds and diffusion barriers …

Septins are cytoskeletal proteins conserved from algae and protists to mammals. A unique
feature of septins is their presence as heteromeric complexes that polymerize into filaments …