Gelsolin: a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Its expression is significantly decreased in many tumors and transformed cell lines. Gelsolin and other proteins including E-cadherin, BRCA, p21WAF, HoxA5, and retinoic acid receptor II are regulated by epigenetic changes in breast cancers. Gelsolin helps mediate the ability of HDAC inhibitors to protect neurons from oxygen/glucose deprivation. Two human isoforms are produced by alternative initiation.
Protein type: Secreted, signal peptide; Actin-binding; Nuclear receptor co-regulator; Motility/polarity/chemotaxis; Secreted
Cellular Component: actin cap; actin cytoskeleton; cortical actin cytoskeleton; cytoplasm; cytoskeleton; cytosol; extracellular region; extracellular space; focal adhesion; lamellipodium; myelin sheath; nucleus; perinuclear region of cytoplasm; plasma membrane; podosome; protein complex; ruffle; sarcoplasm
Molecular Function: actin binding; calcium ion binding; metal ion binding; myosin II binding; protein binding; protein domain specific binding
Biological Process: actin filament capping; actin filament polymerization; actin filament severing; actin nucleation; actin polymerization and/or depolymerization; apoptosis; barbed-end actin filament capping; cell projection organization and biogenesis; negative regulation of virion penetration into host cell; phagocytosis, engulfment; phosphoinositide-mediated signaling; positive regulation of actin nucleation; protein destabilization; regulation of cell adhesion; sequestering of actin monomers; striated muscle atrophy; vesicle-mediated transport
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