Structure, Function, and Evolution of the β‐Thymosin/WH2 (WASP‐Homology2) Actin‐Binding Module

@article{Carlier2007StructureFA,
  title={Structure, Function, and Evolution of the $\beta$‐Thymosin/WH2 (WASP‐Homology2) Actin‐Binding Module},
  author={M. F. Carlier and Maud Hertzog and Dominique Didry and Louis Renault and François-Xavier Cantrelle and Carine van Heijenoort and Marcel Knossow and Eric Guittet},
  journal={Annals of the New York Academy of Sciences},
  year={2007},
  volume={1112}
}
Abstract:  β‐thymosins are acknowledged G‐actin sequesterers. However, in the recent years, the conserved β‐thymosins/WH2 actin‐binding module, has been identified in a large number of proteins that all interact with actin and play diverse functions in cell motility. The functional evolution of the WH2 domain has been approached by a combination of structural and biochemical methods, using thymosin β4 (Tβ4) and Ciboulot, a 3 β‐thymosin repeat protein from Drosophila as models. Ciboulot binds… Expand
How a single residue in individual β‐thymosin/WH2 domains controls their functions in actin assembly
TLDR
The structural mechanisms by which βT/WH2 domains either inhibit assembly by sequestering actin monomers like Thymosin‐β4, or enhance motility by directing polarized filament assembly like Ciboulot βT are revealed. Expand
A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo
TLDR
Normal cell growth and organization depend on the ability of Srv2/CAP to recharge actin monomers, and the WH2 domain plays a central role in this process, and data reveal that while most isolated WH2 domains inhibit nucleotide exchange on actin, WH1 domains in the context of intact proteins can help promote nucleotide Exchange. Expand
The WASP-Homology 2 Domain and Cytoskeleton Assembly
One of the most abundant and functionally diverse actin-binding folds is the WASP homology 2 (WH2 or W) domain. The W domain is found in proteins involved in actin monomer sequestration andExpand
Filament assembly by Spire: key residues and concerted actin binding.
TLDR
This work uses Drosophila Spire (Spir) as a model system to investigate both how tandem WH2 domains can nucleate actin and what differentiates nucleating WH2-containing proteins from their non-nucleating counterparts, and finds that the third WH2 domain in Spir plays a unique role. Expand
In Vitro-Evolved Peptides Bind Monomeric Actin and Mimic Actin-Binding Protein Thymosin-β4.
TLDR
While the F-actin peptides were applied successfully for capturing actin in cell lysates and for imaging, the G-actIn peptides did not bind in the cellular context, most likely due to competition with thymosin-β4 or related endogenous proteins for the same binding site. Expand
Spire and Cordon-bleu: multifunctional regulators of actin dynamics.
TLDR
This work describes how WH2 domains selectively operate in a cellular context to control the dynamics of the actin cytoskeleton and outlines potential methods to gain insight into the functional basis for reported genetic interactions among Spire, profilin and formin. Expand
Actin‐depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics
TLDR
The biochemical functions, cellular roles, and regulation of the five groups of ADF‐H domain proteins are discussed, which are currently incompletely understood. Expand
Presence of WH2 like domain in VgrG-1 toxin of Vibrio cholerae reveals the molecular mechanism of actin cross-linking
TLDR
Actin cross-linking (ACD) domain of VgrG-1 toxin of Type VI secretion in Vibrio cholera has WASP Homology domain 2 (WH2) domain, WH2 is essential for ACD mediated cross- linking and disruption of actin cytoskeleton in the host cell. Expand
Actin filament nucleation and elongation factors – structure–function relationships
  • R. Dominguez
  • Biology, Medicine
  • Critical reviews in biochemistry and molecular biology
  • 2009
TLDR
Structural considerations suggest that NPFs–Arp2/3 complex can also be viewed as a specialized form of tandem W-based nucleator, which is related to WASP-family NPFs. Expand
New players in actin polymerization--WH2-domain-containing actin nucleators.
TLDR
This work summarizes what is currently known about the different molecular mechanisms that Spire, Cordon-Bleu and Leiomodin seem to use and, also, the bacterial counterparts that mimic them (VopF, VopL and TARP). Expand
...
1
2
3
...

References

SHOWING 1-10 OF 43 REFERENCES
The β-Thymosin/WH2 Domain Structural Basis for the Switch from Inhibition to Promotion of Actin Assembly
TLDR
Crystallographic, NMR, and mutagenetic data reveal that the weaker interaction of the C-terminal region of beta-thymosin/WH2 domain with actin accounts for the switch in function from inhibition to promotion of actin assembly. Expand
Structural basis of actin sequestration by thymosin‐β4: implications for WH2 proteins
TLDR
The structure reveals that T β4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tβ4 and profilin is mediated by a minor overlap in binding sites, implying that multiple WH2 motif‐containing proteins will associate longitudinally with actin filaments. Expand
The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins.
TLDR
The crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP are reported, showing that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole cIBoulot forms a complex with two actin monomers. Expand
WH2 domain: a small, versatile adapter for actin monomers
TLDR
The finding of three classes of these proteins: WASP, Srv2/CAP and verprolin/WIP in yeast and animals suggests that the WH2 domain is an ancient actin monomer‐binding motif that existed before the divergence of fungal and animal lineages. Expand
Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly.
TLDR
The crystal structures of complexes of actin with the WH2 domains of WASP, WasP-family verprolin homologous protein, and WASP-interacting protein are described and a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH1, thereby playing a role in filament elongation is suggested. Expand
G‐ to F‐actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin beta 4.
TLDR
The actin binding sites of actobindin and thymosin beta 4, two small polypeptides that inhibit actin polymerization by interacting with monomeric actin, have been localized using peptide mimetics to allow the proposal of a simple model for G‐ to F‐actin modulation. Expand
Coupling of Folding and Binding of Thymosin β4 upon Interaction with Monomeric Actin Monitored by Nuclear Magnetic Resonance*
TLDR
It is shown here that the whole backbone of thymosin β4 is highly affected upon binding to G-actin, showing that the backbone of the peptide is not in close proximity to segment 42-47 of actin. Expand
A CapG gain‐of‐function mutant reveals critical structural and functional determinants for actin filament severing
TLDR
It is concluded that efficient severing utilizes two actin monomer‐binding sites, and that the length of the WH2‐containing segment is a critical functional determinant for severing. Expand
Structural basis for the actin-binding function of missing-in-metastasis.
TLDR
Comparison of the structures of MIM's IMD and that of its WH2 bound to actin reveals that the membrane binding surfaces of the two domains have opposite curvatures, which may determine the type of curvature of the interacting membrane. Expand
Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family.
TLDR
It is shown that actobindin has the same biochemical properties as the Drosophila or Caenorhabditis elegans homologous protein that consists of three beta-thymosin repeats, defining a new family of actin-binding proteins that behave as functional homologs of profilin. Expand
...
1
2
3
4
5
...