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. Note: This description may include information from UniProtKB.
Protein type: Actin binding protein; Motility/polarity/chemotaxis; Secreted, signal peptide; Secreted; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 9q33
Cellular Component: ruffle; protein complex; lamellipodium; perinuclear region of cytoplasm; extracellular region; cytosol; actin cytoskeleton
Molecular Function: protein binding; calcium ion binding; actin binding
Biological Process: regulation of cell adhesion; actin filament severing; phosphoinositide-mediated signaling; apoptosis; vesicle-mediated transport; response to ethanol; actin filament polymerization; tissue regeneration; response to folic acid; oligodendrocyte development; barbed-end actin filament capping; aging; cell structure disassembly during apoptosis
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.