ArticleThe Journal of biological chemistry2016
Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 22 citations in OpenAlex.
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- Deconvolution Analysis of G and F-Actin Unfolding: Insights into the Thermal Stability and Structural Modifications Induced by PACAP.International journal of molecular sciences · 2025Article
- Exploring the Role of Neuropeptide PACAP in Cytoskeletal Function Using Spectroscopic Methods.International journal of molecular sciences · 2024Article
- Peripheral thickening of the sarcomeres and pointed end elongation of the thin filaments are both promoted by SALS and its formin interaction partners.PLoS genetics · 2024Article
- Drosophila Tropomodulin is required for multiple actin-dependent processes within developing myofibers.Development (Cambridge, England) · 2023Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin.The Journal of biological chemistry · 2021Article
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
- Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion.Nature communications · 2019Article
- Article
- Tropomyosins Regulate the Severing Activity of Gelsolin in Isoform-Dependent and Independent Manners.Biophysical journal · 2018Article
- The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics.The Journal of biological chemistry · 2017Article
- Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.PloS one · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Drosophila melanogaster sarcomere length short (SALS) is a recently identified Wiskott-Aldrich syndrome protein homology 2 (WH2) domain protein involved in skeletal muscle thin filament regulation. SALS was shown to be important for the establishment of the proper length and organization of sarcomeric actin filaments. Here, we present the first detailed characterization of the biochemical activities of the tandem WH2 domains of SALS (SALS-WH2). Our results revealed that SALS-WH2 binds both monomeric and filamentous actin and shifts the monomer-filament equilibrium toward the monomeric actin. In addition, SALS-WH2 can bind to but fails to depolymerize phalloidin- or jasplakinolide-bound actin filaments. These interactions endow SALS-WH2 with the following two major activities in the regulation of actin dynamics: SALS-WH2 sequesters actin monomers into non-polymerizable complexes and enhances actin filament disassembly by severing, which is modulated by tropomyosin. We also show that profilin does not influence the activities of the WH2 domains of SALS in actin dynamics. In conclusion, the tandem WH2 domains of SALS are multifunctional regulators of actin dynamics. Our findings suggest that the activities of the WH2 domains do not reconstitute the presumed biological function of the full-length protein. Consequently, the interactions of the WH2 domains of SALS with actin must be tuned in the cellular context by other modules of the protein and/or sarcomeric components for its proper functioning.
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