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Spire proteins, such as SPIRE1, are highly conserved between species. Additionally we are shipping Spire Homolog 1 (Drosophila) Antibodies (26) and many more products for this protein.
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Spire-1 is specifically recruited at invadosomes and is part of a multi-molecular complex containing Src kinase, the formin mDia1 and actin.
analysis of the molecular basis of the Spir1/formin-2 interaction
Spire1 and Spire2 (show SPIRE2 Proteins) drive two critical steps of asymmetric oocyte division.
By analyzing the expression of the spir-1 gene it was shown that spir-1 and formin-2 have a nearly identical expression pattern during mouse embryogenesis and in the adult brain.
Data suggest formin homology domain (FH2) of Fmn2 binds actin at filament barbed end as weak capper and plays a role in displacing WASP homology domain 2 (WH2) domains of Spire-1 from actin; competitive binding of Fmn2 vs Spire-1 aids actin assembly.
This DNA damage-induced nuclear actin assembly requires two biologically and physically linked nucleation factors: Formin-2 and Spire-1/Spire-2.
The authors propose Spire1C isoform cooperates with INF2 to regulate actin assembly at endoplasmic reticulum-mitochondrial contacts.
Spire recruits Fmn2 and facilitates its association with actin filaments barbed ends.
The multifunctional character of the WH2 domains allows Spire to sequester four G-actin (show ACTB Proteins) subunits binding cooperatively in a tight SA(4) complex and to nucleate, sever, and cap filaments at their barbed ends.
both mammalian Spir proteins, Spir-1 and Spir-2, interact with mammalian Fmn subgroup proteins formin-1 and formin-2
Spire proteins, such as SPIRE1, are highly conserved between species. They belong to the family of Wiskott-Aldrich homology region-2 (WH2) proteins, which are involved in actin organization (Kerkhoff et al., 2001
protein spire homolog 1
, spire homolog 1
, spire actin nucleation factor 1
, spire family actin nucleation factor 1