Swiprosin-1 Is a Novel Actin Bundling Protein That Regulates Cell Spreading and Migration

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Swiprosin-1 Is a Novel Actin Bundling Protein That Regulates Cell Spreading and Migration

Public Library of Science
DOI: 10.1371/journal.pone.0071626
  • Biology
  • Biochemistry
  • Proteins
  • Developmental Biology
  • Morphogenesis
  • Cell Migration
  • Cytoskeleton
  • Research Article
  • Extracellular Matrix
  • Cell Physiology
  • Cytoskeletal Proteins
  • Molecular Cell Biology
  • Anatomy And Physiology
  • Cellular Structures
  • Extracellular Matrix Adhesions


Protein functions are often revealed by their localization to specialized cellular sites. Recent reports demonstrated that swiprosin-1 is found together with actin and actin-binding proteins in the cytoskeleton fraction of human mast cells and NK-like cells. However, direct evidence of whether swiprosin-1 regulates actin dynamics is currently lacking. We found that swiprosin-1 localizes to microvilli-like membrane protrusions and lamellipodia and exhibits actin-binding activity. Overexpression of swiprosin-1 enhanced lamellipodia formation and cell spreading. In contrast, swiprosin-1 knockdown showed reduced cell spreading and migration. Swiprosin-1 induced actin bundling in the presence of Ca2+, and deletion of the EF-hand motifs partially reduced bundling activity. Swiprosin-1 dimerized in the presence of Ca2+ via its coiled-coil domain, and a lysine (Lys)-rich region in the coiled-coil domain was essential for regulation of actin bundling. Consistent with these observations, mutations of the EF-hand motifs and coiled-coil region significantly reduced cell spreading and lamellipodia formation. We provide new evidence of how swiprosin-1 influences cytoskeleton reorganization and cell spreading.

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