Structural highlights
Function
ARP3_BOVIN Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis (By similarity).
Publication Abstract from PubMed
The Arp2/3 complex mediates formation of complex cellular structures such as lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is precisely controlled by over a dozen regulators, yet the structural mechanism by which regulators interact with the complex is unknown. GMF is a recently discovered regulator of the Arp2/3 complex that can inhibit nucleation and disassemble branches. We solved the structure of the 240-kDa assembly of Mus musculus GMF and Bos taurus Arp2/3 complex and found that GMF binds the barbed end of Arp2, overlapping with the proposed binding site of WASP-family proteins. The structure suggests that GMF can bind branch junctions in the manner that cofilin binds filament sides, consistent with a modified cofilin-like mechanism for debranching by GMF. The GMF-Arp2 interface reveals how the ADF-H actin-binding domain in GMF is exploited to specifically recognize Arp2/3 complex and not actin.
Structural basis for regulation of Arp2/3 complex by GMF.,Luan Q, Nolen BJ Nat Struct Mol Biol. 2013 Jul 28. doi: 10.1038/nsmb.2628. PMID:23893131[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luan Q, Nolen BJ. Structural basis for regulation of Arp2/3 complex by GMF. Nat Struct Mol Biol. 2013 Jul 28. doi: 10.1038/nsmb.2628. PMID:23893131 doi:10.1038/nsmb.2628
