3r7g

Structural highlights

Function

[SPIR1_HUMAN] Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis.^{[1] [2]} [FMN2_HUMAN] Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.^{[3] [4]}

References

1. ↑ Kerkhoff E, Simpson JC, Leberfinger CB, Otto IM, Doerks T, Bork P, Rapp UR, Raabe T, Pepperkok R. The Spir actin organizers are involved in vesicle transport processes. Curr Biol. 2001 Dec 11;11(24):1963-8. PMID:11747823
2. ↑ Pfender S, Kuznetsov V, Pleiser S, Kerkhoff E, Schuh M. Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division. Curr Biol. 2011 Jun 7;21(11):955-60. doi: 10.1016/j.cub.2011.04.029. Epub 2011, May 27. PMID:21620703 doi:http://dx.doi.org/10.1016/j.cub.2011.04.029
3. ↑ Peng KW, Liou YM. Differential role of actin-binding proteins in controlling the adipogenic differentiation of human CD105-positive Wharton's Jelly cells. Biochim Biophys Acta. 2012 Apr;1820(4):469-81. doi: 10.1016/j.bbagen.2012.01.014., Epub 2012 Feb 8. PMID:22330775 doi:http://dx.doi.org/10.1016/j.bbagen.2012.01.014
4. ↑ Yamada K, Ono M, Perkins ND, Rocha S, Lamond AI. Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21. Mol Cell. 2013 Mar 7;49(5):922-33. doi: 10.1016/j.molcel.2012.12.023. Epub 2013, Jan 31. PMID:23375502 doi:http://dx.doi.org/10.1016/j.molcel.2012.12.023