ArticleJournal of molecular biology2011
Mechanism of the Ca²+-dependent interaction between S100A4 and tail fragments of nonmuscle myosin heavy chain IIA.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Impairment of non-muscle myosin IIA in human CD4+ T cells contributes to functional deficits in the elderly.Cellular & molecular immunology · 2012Trial
- Downregulation of PIEZO1 Activity Promotes Breast Cancer Cell Survival under Shear Stress by Modulating β-Catenin and BCL2.Cancer research communications · 2026Article
- Non-muscle myosin 2 at a glance.Journal of cell science · 2023Review
- Article
- Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes.Frontiers in molecular biosciences · 2021Review
- Direct interaction of metastasis-inducing S100P protein with tubulin causes enhanced cell migration without changes in cell adhesion.The Biochemical journal · 2020Article
- Matrigel patterning reflects multicellular contractility.PLoS computational biology · 2019Article
- MYH9 Aggregation Induced by Direct Interaction With PRRSV GP5 Ectodomain Facilitates Viral Internalization by Permissive Cells.Frontiers in microbiology · 2019Article
- Constrained α-Helical Peptides as Inhibitors of Protein-Protein and Protein-DNA Interactions.Biomedicines · 2018Review
- Multiple S100 protein isoforms and C-terminal phosphorylation contribute to the paralog-selective regulation of nonmuscle myosin 2 filaments.The Journal of biological chemistry · 2018Article
- S100A4 in cancer progression and metastasis: A systematic review.Oncotarget · 2017Review
- Local pulsatile contractions are an intrinsic property of the myosin 2A motor in the cortical cytoskeleton of adherent cells.Molecular biology of the cell · 2017Article
- Myosin II isoform co-assembly and differential regulation in mammalian systems.Experimental cell research · 2015Review
- Life without double-headed non-muscle myosin II motor proteins.Frontiers in chemistry · 2014Review
- Structure of the S100A4/myosin-IIA complex.BMC structural biology · 2013Article
- Progressive impairment of muscle regeneration in muscleblind-like 3 isoform knockout mice.Human molecular genetics · 2013Article
- Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility.Biochemistry · 2012Article
- S100A4 in esophageal cancer: is this the one to blame?World journal of gastroenterology · 2012Article
- S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration.The Journal of biological chemistry · 2012Article
- Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
The interaction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin heavy chain IIA has been studied by equilibrium and kinetic methods. Using site-directed mutants, we conclude that Ca(2+) binds to the EF2 domain of S100A4 with micromolar affinity and that the K(d) value for Ca(2+) is reduced by several orders of magnitude in the presence of myosin target fragments. The reduction in K(d) results from a reduced dissociation rate constant (from 16 s(-1) to 0.3 s(-1) in the presence of coiled-coil fragments) and an increased association rate constant. Using peptide competition assays and NMR spectroscopy, we conclude that the minimal binding site on myosin heavy chain IIA corresponds to A1907-G1938; therefore, the site extends beyond the end of the coiled-coil region of myosin. Electron microscopy and turbidity assays were used to assess myosin fragment filament disassembly by S100A4. The latter assay demonstrated that S100A4 binds to the filaments and actively promotes disassembly rather than just binding to the myosin monomer and displacing the equilibrium. Quantitative modelling of these in vitro data suggests that S100A4 concentrations in the micromolar region could disassemble myosin filaments even at resting levels of cytoplasmic [Ca(2+)]. However, for Ca(2+) transients to be effective in further promoting dissociation, the elevated Ca(2+) signal must persist for tens of seconds. Fluorescence recovery after photobleaching of A431/SIP1 cells expressing green fluorescent protein-myosin IIA, immobilised on fibronectin micropatterns to control stress fibre location, yielded a recovery time constant of around 20 s, consistent with in vitro data.
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