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Drosophila Spire is an actin nucleation factor
- Source :
- Nature. 433:382-388
- Publication Year :
- 2005
- Publisher :
- Springer Science and Business Media LLC, 2005.
-
Abstract
- The actin cytoskeleton is essential for many cellular functions including shape determination, intracellular transport and locomotion. Previous work has identified two factors--the Arp2/3 complex and the formin family of proteins--that nucleate new actin filaments via different mechanisms. Here we show that the Drosophila protein Spire represents a third class of actin nucleation factor. In vitro, Spire nucleates new filaments at a rate that is similar to that of the formin family of proteins but slower than in the activated Arp2/3 complex, and it remains associated with the slow-growing pointed end of the new filament. Spire contains a cluster of four WASP homology 2 (WH2) domains, each of which binds an actin monomer. Maximal nucleation activity requires all four WH2 domains along with an additional actin-binding motif, conserved among Spire proteins. Spire itself is conserved among metazoans and, together with the formin Cappuccino, is required for axis specification in oocytes and embryos, suggesting that multiple actin nucleation factors collaborate to construct essential cytoskeletal structures.
- Subjects :
- Molecular Sequence Data
Arp2/3 complex
macromolecular substances
Animals
Drosophila Proteins
Amino Acid Sequence
Axis specification
Protein Structure, Quaternary
Cytoskeleton
Actin nucleation
Binding Sites
Multidisciplinary
biology
Microfilament Proteins
Actin remodeling
Actin cytoskeleton
Actins
Protein Structure, Tertiary
Cell biology
Actin Cytoskeleton
Drosophila melanogaster
Multiprotein Complexes
Formins
biology.protein
MDia1
Protein Binding
Subjects
Details
- ISSN :
- 14764687 and 00280836
- Volume :
- 433
- Database :
- OpenAIRE
- Journal :
- Nature
- Accession number :
- edsair.doi.dedup.....e5d5da4a9d8a08c7a87fcefce4e05b8b