Related Experiment Video
Updated: May 12, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
Published on: June 23, 2022
The septin family of GTPases: architecture and dynamics
Christine S Weirich1, Jan P Erzberger, Yves Barral
1Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland.
Abstract:
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 organization and membrane-remodelling events. One factor that is crucial for their functions is the ordered assembly of individual septins into oligomeric core complexes that, in turn, form higher-order structures such as filaments, rings and gauzes. The molecular details of these interactions and the mechanism by which septin-complex assembly is regulated have remained elusive. Recently, the first detailed structural views of the septin core have emerged, and these, along with studies of septin dynamics in vivo, have provided new insight into septin-complex assembly and septin function in vivo.
More Related Videos
Related Concept Videos
GTPases and their Regulation
Large G-proteins, also known...
Septins
The Contractile Ring
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
GTPases and their Regulation
Large G-proteins, also known...
Role of Septins
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:

