Structural basis for regulation of Arp2/3 complex by GMF
Copyright policy )Structural basis for regulation of Arp2/3 complex by GMF
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.
- University of Oregon United States
Glia Maturation Factor, Models, Molecular, Sequence Homology, Amino Acid, Molecular Sequence Data, Crystallography, X-Ray, Article, Actin-Related Protein 2-3 Complex, Actins, Recombinant Proteins, Wiskott-Aldrich Syndrome Protein Family, Mice, Protein Subunits, Multiprotein Complexes, Animals, Cattle, Protein Interaction Domains and Motifs, Amino Acid Sequence
Glia Maturation Factor, Models, Molecular, Sequence Homology, Amino Acid, Molecular Sequence Data, Crystallography, X-Ray, Article, Actin-Related Protein 2-3 Complex, Actins, Recombinant Proteins, Wiskott-Aldrich Syndrome Protein Family, Mice, Protein Subunits, Multiprotein Complexes, Animals, Cattle, Protein Interaction Domains and Motifs, Amino Acid Sequence
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