Control of actin assembly at filament ends.
Actin filament polymerization involves exchange of subunits of filament ends, which can be controlled in vitro and in vivo by other proteins that bind actin filaments and inhibit subunit addition or loss at the ends. Proteins that bind to the barbed end, including capping protein, the gelsolin super-family, tensin, and profilin are discussed, as are proteins that bind to the pointed end, including tropomodulin and spectrin/band 4.1. Some proteins that bind along the sides of filaments and influence assembly at ends are also discussed. Functional roles in vivo are emphasized.
Schafer
D A
DA
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Cooper
J A
JA
D000199:Actins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D017985:Dalteparin / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D018260:Gelsolin / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism; D008840:Microfilament Proteins / Q000378:metabolism*; D009479:Neuropeptides; D051304:Profilins; D015800:Protozoan Proteins; D013049:Spectrin / Q000378:metabolism; D000070876:Tensins; D051348:Tropomodulin
D000199:Actins; D002352:Carrier Proteins; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins; D018260:Gelsolin; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008840:Microfilament Proteins; D009479:Neuropeptides; C495738:PFN1 protein, human; D051304:Profilins; D015800:Protozoan Proteins; C495829:TMOD1 protein, human; D000070876:Tensins; D051348:Tropomodulin; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; C065395:scinderin; C036571:severin protein, Dictyostelium; C026615:villin; D013049:Spectrin; D017985:Dalteparin