Structural insights into actin-binding, branching and bundling proteins.
Structural advances in our understanding of the functions of the actin cytoskeleton have come from diverse sources. On the one hand, the determination of the structure of a bacterial actin-like protein MreB reveals the prokaryotic origins of the actin cytoskeleton, whereas on the other, cryo-electron microscopy and crystallography have yielded reconstructions of many actin crosslinking, regulatory and binding proteins in complex with F-actin. Not least, a high-resolution structure of the Arp2/3 complex and a reconstruction with F-actin provides considerable insight into the eukaryotic machinery, vital for the formation of new F-actin barbed ends, a prerequisite for rapid actin polymerisation involved in cell shape change and motility.
Winder
Steven J
SJ
Institute of Biomedical and Life Sciences, Cell Biology Group, Davidson Building, University of Glasgow, Glasgow G12 8QQ, Scotland, UK. s.winder@bio.gla.ac.uk
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D051377:Actin-Related Protein 2; D000818:Animals; D003598:Cytoskeletal Proteins / Q000378:metabolism / Q000648:ultrastructure; D003599:Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D046911:Macromolecular Substances; D008840:Microfilament Proteins / Q000378:metabolism* / Q000648:ultrastructure; D020836:Protein Structure, Quaternary / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology
C495926:ACTR2 protein, human; D051377:Actin-Related Protein 2; D003598:Cytoskeletal Proteins; D046911:Macromolecular Substances; D008840:Microfilament Proteins; C052523:actin filament bundling proteins