ArticleMolecular biology of the cell2004
TetraThymosinbeta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 36 citations in OpenAlex.
- Embryogenesis in the parasitic nematode Heterodera glycines is independent of host-derived hatching stimulation.BMC developmental biology · 2017Article
- Thymosin β4 and tissue transglutaminase. Molecular characterization of cyclic thymosin β4.The protein journal · 2013Article
- How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly.The EMBO journal · 2012Article
- Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation.Journal of molecular biology · 2010Article
- The homolog of Ciboulot in the termite (Hodotermopsis sjostedti): a multimeric beta-thymosin involved in soldier-specific morphogenesis.BMC developmental biology · 2010Article
- Proteomic analysis of post-translational modifications in conditioned Hermissenda.Neuroscience · 2010Article
- Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner.Cell motility and the cytoskeleton · 2006Article
- Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Actin filament nucleation and elongation factors--structure-function relationships.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
8 authors at 2 institutions in 2 countries.
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Abstract
Generating specific actin structures via controlled actin polymerization is a prerequisite for eukaryote development and reproduction. We here report on an essential Caenorhabditis elegans protein tetraThymosinbeta expressed in developing neurons and crucial during oocyte maturation in adults. TetraThymosinbeta has four repeats, each related to the actin monomer-sequestering protein thymosinbeta 4 and assists in actin filament elongation. For homologues with similar multirepeat structures, a profilin-like mechanism of ushering actin onto filament barbed ends, based on the formation of a 1:1 complex, is proposed to underlie this activity. We, however, demonstrate that tetraThymosinbeta binds multiple actin monomers via different repeats and in addition also interacts with filamentous actin. All repeats need to be functional for attaining full activity in various in vitro assays. The activities on actin are thus a direct consequence of the repeated structure. In containing both G- and F-actin interaction sites, tetraThymosinbeta may be reminiscent of nonhomologous multimodular actin regulatory proteins implicated in actin filament dynamics. A mutation that suppresses expression of tetraThymosinbeta is homozygous lethal. Mutant organisms develop into adults but display a dumpy phenotype and fail to reproduce as their oocytes lack essential actin structures. This strongly suggests that the activity of tetraThymosinbeta is of crucial importance at specific developmental stages requiring actin polymerization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.