Sulfiredoxin Redox-Sensitive Interaction with S100A4 and Non-Muscle Myosin IIA Regulates Cancer Cell Motility
Copyright policy )Sulfiredoxin Redox-Sensitive Interaction with S100A4 and Non-Muscle Myosin IIA Regulates Cancer Cell Motility
Sulfiredoxin (Srx) is a redox active protein that participates in the reduction of oxidized cysteine residues. Here we identify a novel function of Srx through its specific binding to S-glutathionylated S100A4 affecting its interaction with non-muscle myosin (NMIIA), thereby modulating the effect of S100A4 on NMIIA function and impacting cell adhesion and migration. Srx forms a complex with S100A4 (and has stronger affinity for S-glutathionylated S100A4), regulates its activity, and mediates redox regulation of the interaction of S100A4 with NMIIA. The consequence of this regulation is microfilament remodeling and altered cellular motility and adhesion. Srx-overexpressing cells had reduced levels of adhesion, decreased levels of Tyr(397)-phosphorylated focal adhesion kinase, and increased cell motility in wound healing assays. These results describe a novel redox-sensitive role for Srx in mediating complex protein interactions with plausible consequences for cancer cell motility.
- Medical University of South Carolina United States
Models, Molecular, Lung Neoplasms, Nonmuscle Myosin Type IIA, S100 Proteins, Glutathione, Immunohistochemistry, Actins, Cell Movement, Carcinoma, Non-Small-Cell Lung, Cell Line, Tumor, Protein Interaction Mapping, Cell Adhesion, Humans, Oxidoreductases Acting on Sulfur Group Donors, S100 Calcium-Binding Protein A4, Oxidation-Reduction, Protein Binding
Models, Molecular, Lung Neoplasms, Nonmuscle Myosin Type IIA, S100 Proteins, Glutathione, Immunohistochemistry, Actins, Cell Movement, Carcinoma, Non-Small-Cell Lung, Cell Line, Tumor, Protein Interaction Mapping, Cell Adhesion, Humans, Oxidoreductases Acting on Sulfur Group Donors, S100 Calcium-Binding Protein A4, Oxidation-Reduction, Protein Binding
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