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Control of actin assembly at filament ends.
- Source :
-
Annual review of cell and developmental biology [Annu Rev Cell Dev Biol] 1995; Vol. 11, pp. 497-518. - Publication Year :
- 1995
-
Abstract
- 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.
- Subjects :
- Actins chemistry
Animals
Carrier Proteins metabolism
Dalteparin metabolism
Fungal Proteins metabolism
Gelsolin metabolism
Humans
Macromolecular Substances
Membrane Proteins metabolism
Profilins
Spectrin metabolism
Tensins
Tropomodulin
Actins metabolism
Actins ultrastructure
Contractile Proteins
Cytoskeletal Proteins
Microfilament Proteins metabolism
Neuropeptides
Protozoan Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 1081-0706
- Volume :
- 11
- Database :
- MEDLINE
- Journal :
- Annual review of cell and developmental biology
- Publication Type :
- Academic Journal
- Accession number :
- 8689567
- Full Text :
- https://doi.org/10.1146/annurev.cb.11.110195.002433