Portal de Periódicos da CAPES

Gelsolin: Calcium‐ and polyphosphoinositide‐regulated actin‐ modulating protein

1987; Wiley; Volume: 7; Issue: 4 Linguagem: Inglês

10.1002/bies.950070409

1521-1878

H L Yin,

Advanced Fluorescence Microscopy Techniques

Abstract Receptor‐mediated stimulation induces massive actin polymerization and cyto‐skeletal reorganization. The activity of a potent actin‐modulating protein, gelsolin, is regulated both by Ca 2+ and polyphos‐phoinositides, and it may have a pivotal role in restructuring the actin cytoskeleton in response to agonist stimulation. Structure‐function analysis of gelsolin has (1) indicated that its NH 2 ‐terminal half is primarily responsible for modulating actin filament length and polymerization; and (2) elucidated mechanisms by which Ca 2+ and phospholipids may regulate such functions. Gelsolin is functionally and structurally similar to villin, another Ca 2+ ‐activated actin‐severing protein found in microvilli, suggesting that gelsolin may be a prototype of this family of actin‐modulating proteins. A molecular variant of gelsolin is secreted and may be involved in the clearance of actin filaments released during tissue damage. The two forms of gelsolin are encoded by a single gene, and distinct messages are derived by alternative message splicing.