The Comparison of β-Thymosin Homologues Among Metazoa Supports an Arthropod-Nematode Clade

Manuel, Michaël; Kruse, Michael; Müller, Wernér E.G.; Parco, Yannick Le

doi:10.1007/s002390010100

Cited by 89 publications

(38 citation statements)

References 22 publications

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“…Other assembly or prediction errors, which are likely to occur at random, are unlikely to lead to the pattern of greater than expected parallel gene family loss observed here (Tables 1 and 2). The phylogenetic position of nematodes has been controversial in recent years (Aguinaldo et al 1997;Hausdorf 2000;Manuel et al 2000;Blair et al 2002;Mallet et al 2004). According to the Ecdysozoa hypothesis, nemotodes cluster with arthropods and related phyla (Aguinaldo et al 1997).…”

Section: Discussionmentioning

confidence: 99%

Shedding Genomic Ballast: Extensive Parallel Loss of Ancestral Gene Families in Animals

Hughes

Friedman

2004

J Mol Evol

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Abstract. Loss of ancestral gene families has played an important role in genomic specialization in animals. An examination of the pattern of gene family loss in completely sequenced animal genomes revealed that the same gene families have been lost independently in different lineages to a far greater extent than expected if gene loss occurred at random. This result implies that certain ancestral gene families-and thus the biological functions they encode-have been more expendable than others over the radiation of the animal phyla.

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Section: Discussionmentioning

confidence: 99%

Shedding Genomic Ballast: Extensive Parallel Loss of Ancestral Gene Families in Animals

Hughes

Friedman

2004

J Mol Evol

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“…The multimeric beta-thymosin gene found in flies and nematode worms (Manuel et al 2000) has been shown not to be a synapomorphy of the Ecdysozoa ( Telford 2004).…”

Section: The Ecdysozoa Is a Monophyletic Groupmentioning

confidence: 99%

The evolution of the Ecdysozoa

Telford

Bourlat

Economou

et al. 2008

Phil. Trans. R. Soc. B

190

121

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Ecdysozoa is a clade composed of eight phyla: the arthropods, tardigrades and onychophorans that share segmentation and appendages and the nematodes, nematomorphs, priapulids, kinorhynchs and loriciferans, which are worms with an anterior proboscis or introvert. Ecdysozoa contains the vast majority of animal species and there is a great diversity of body plans among both living and fossil members. The monophyly of the clade has been called into question by some workers based on analyses of whole genome datasets. We review the evidence that now conclusively supports the unique origin of these phyla. Relationships within Ecdysozoa are also controversial and we discuss the molecular and morphological evidence for a number of monophyletic groups within this superphylum.

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“…In metazoa, T␤ proteins consist of a single copy of T␤, with T␤4 as the prototypical member of this family. However, in arthropoda and nematoda, T␤ occurs only in the form of tandem repeats, such as in Drosophila ciboulot and C. elegans tetraT␤ (24). In contrast, WH2 is found from yeast to human in the form of single or multiple copies within large multidomain proteins.…”

Section: Control Of Actin Nucleotide Exchange By Wh2 and T␤mentioning

confidence: 99%

Actin-bound structures of Wiskott–Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly

Chéreau

Kerff

Graceffa

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

237

375

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Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) is a small and widespread actin-binding motif. In the WASP family, WH2 plays a role in filament nucleation by Arp2͞3 complex. Here we describe the crystal structures of complexes of actin with the WH2 domains of WASP, WASP-family verprolin homologous protein, and WASP-interacting protein. Despite low sequence identity, WH2 shares structural similarity with the N-terminal portion of the actin monomer-sequestering thymosin ␤ domain (T␤). We show that both domains inhibit nucleotide exchange by targeting the cleft between actin subdomains 1 and 3, a common binding site for many unrelated actin-binding proteins. Importantly, WH2 is significantly shorter than T␤ but binds actin with Ϸ10-fold higher affinity. WH2 lacks a C-terminal extension that in T␤4 becomes involved in monomer sequestration by interfering with intersubunit contacts in F-actin. Owing to their shorter length, WH2 domains connected in tandem by short linkers can coexist with intersubunit contacts in F-actin and are proposed to function in filament nucleation by lining up actin subunits along a filament strand. The WH2-central region of WASP-family proteins is proposed to function in an analogous way by forming a special class of tandem repeats whose function is to line up actin and Arp2 during Arp2͞3 nucleation. The structures also suggest a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH2, thereby playing a role in filament elongation.x-ray crystallography ͉ isothermal titration calorimetry ͉ nucleotide exchange T he actin cytoskeleton plays an essential role in many cellular functions, including intracellular transport and the control of cell shape and polarity (1). In the cell, a vast number of actin-binding proteins (ABPs) direct the location, rate, and timing for actin assembly into different structures, such as filopodia, lamellipodia, stress fibers, and focal adhesions. ABPs are commonly multidomain proteins, containing signaling domains and structurally conserved actin-binding motifs. One of the most abundant actin-binding motifs is Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) (2). The hematopoietic-specific protein, WASP, and its ubiquitously expressed ortholog N-WASP form part of a family that also includes the three WASP-family verprolin homologous protein (WAVE͞SCAR) isoforms: WAVE1, WAVE2, and WAVE3 (1, 3). Members of this family activate Arp2͞3-dependent actin nucleation and branching in response to signals mediated by Rho-family GTPases. Although the domain structure of these proteins varies, reflecting different modes of regulation, they all share a common C-terminal WH2 central-acidic region (CA region) (Fig. 1A), which constitutes the smallest fragment necessary for Arp2͞3 activation (4). WH2 is also present in members of the WASP-interacting protein (WIP) family, which form complexes with WASP͞N-WASP and modulate their functions in vivo (5, 6). Members of this family include ...

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The Comparison of β-Thymosin Homologues Among Metazoa Supports an Arthropod-Nematode Clade

Cited by 89 publications

References 22 publications

Shedding Genomic Ballast: Extensive Parallel Loss of Ancestral Gene Families in Animals

Shedding Genomic Ballast: Extensive Parallel Loss of Ancestral Gene Families in Animals

The evolution of the Ecdysozoa

Actin-bound structures of Wiskott–Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly

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