Microtubule-associated proteins (MAPs) were initially discovered as proteins that bind to
and stabilize microtubules. Today, an ever-growing number of MAPs reveals a more …

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

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 …

The establishment of cell polarity is critical for the development of many organisms and for
the function of many cell types. A large number of studies of diverse organisms from yeast to …

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 …

Septins are a family of GTP-binding proteins implicated in mammalian cell division. Most
studies examining the role of septins in this process have treated the family as a whole, thus …

Septins, a highly conserved family of GTP-binding proteins, were originally identified in a
genetic screen for S. cerevisiae mutants defective in cytokinesis [1, 2]. In yeast, septins …

Human septins comprise a family of 13 genes that encode for> 30 protein isoforms with
ubiquitous and tissue-specific expressions. Septins are GTP-binding proteins that assemble …

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 …

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