|Title||The state of the filament|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Aguda, AH, Burtnick, LD, Robinson, RC|
|Type of Article||Review|
|Keywords||actin filament, ACTIN-FILAMENT, ACTIVATION, ALDRICH-SYNDROME PROTEIN, arp2/3, ARP2/3 COMPLEX, BETA-ACTIN, CRYSTAL-STRUCTURE, DOMAIN, gelsolin, STRUCTURAL BASIS, STRUCTURE, WASp, WH2|
Movement is a defining characteristic of life. Macroscopic motion is driven by the dynamic interactions of myosin with actin filaments in muscle. Directed polymerization of actin behind the advancing membrane of a eukaryotic cell generates microscopic movement. Despite the fundamental importance of actin in these processes, the structure of the actin filament remains unknown. The Holmes model of the actin filament was published 15 years ago, and although it has been widely accepted, no high-resolution structural data have yet confirmed its veracity. Here, we review the implications of recently determined structures of F-actin-binding proteins for the structure of the actin filament and suggest a series of in silico tests for actin-filament models. We also review the significance of these structures for the arp2/3-mediated branched filament.
|URL||<Go to ISI>://000227297000009|