Elias T. Spiliotis

The actin and microtubule cytoskeletons comprise a variety of networks with distinct architectures, dynamics and protein composition. A fundamental question in eukaryotic cell biology is how these networks are spatially and temporally controlled, so they are positioned in the right intracellular places at the right time. While significant progress has been made in understanding the self-assembly of actin and microtubule networks, less is known about how they are patterned and regulated in a site-specific manner. In mammalian systems, septins are a large family of GTP-binding proteins that multimerize into higher-order structures, which associate with distinct subsets of actin filaments and microtubules, as well as membranes of specific curvature and lipid composition. Recent studies have shed more light on how septins interact with actin and microtubules, and raised the possibility that the cytoskeletal topology of septins is determined by their membrane specificity. Importantly, new functions have emerged for septins regarding the generation, maintenance and positioning of cytoskeletal networks with distinct organization and biochemical makeup. This Review presents new and past findings, and discusses septins as a unique regulatory module that instructs the local differentiation and positioning of distinct actin and microtubule networks.