The first identified members of the septin family of cytoskeletal GTPases were originally
discovered in the budding yeast Saccharomyces cerevisiae as crucial regulators of mother …

Septins are a family of conserved cytoskeletal GTPases with unique heteropolymerization
properties and diverse physiological functions (reviewed in Mostowy and Cossart, 2012) …

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

Septins are a family of proteins highly conserved in eukaryotes that have been under
intense scrutiny lately because they appear to comprise a novel component of the …

Septins embrace a large family of proteins highly conserved among eukaryotic species.
They were originally identified in budding yeast in the early 1970s as proteins essential for …

Septins are guanosine triphosphate (GTP)-binding proteins that assemble into hetero-
oligomeric complexes and form nonpolar filaments that associate with cellular membranes …

Background Septins belong to the GTPase superclass of proteins and have been
functionally implicated in cytokinesis and the maintenance of cellular morphology. They are …

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 …

Since the initial discovery of septin family GTPases, the understanding of their molecular
organization and cellular roles keeps being refined. Septins have been involved in many …

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 …