Tropomodulins: life at the slow end.
Dynamic exchange of actin monomers at filament ends is crucial for the functional architecture of many cytoskeletal-dependent processes. Recent evidence indicates that tropomodulins (Tmods), a conserved family of actin-capping proteins that bind to the pointed (slow-growing) end of actin filaments, regulate a variety of actin structures, including dynamic actin networks found in some motile cells. Actin structures that are more stable, such as sarcomeric thin filaments, require capping by Tmods to specify filament lengths and to provide filament stability. Here, we discuss the functional differences between the capping of pointed and barbed ends within the context of these actin-filament systems, and how Tmods uniquely contribute to their regulation and organization.
Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. bfischer@scripps.edu
Robert S
RS
Fischer
Velia M
VM
Fowler
D008841:Actin Cytoskeleton / Q000737:chemistry / Q000502:physiology; D000199:Actins / Q000737:chemistry / Q000502:physiology; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000502:physiology*; D011485:Protein Binding; D051348:Tropomodulin
D000199:Actins; D002352:Carrier Proteins; D008840:Microfilament Proteins; C495829:TMOD1 protein, human; D051348:Tropomodulin