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Abstract
Gelsolin plays a critical role in regulating the dynamic changes in the actin cytoskeleton. The actin-binding protein was first discovered as a modulator of the transformation of cytoplasm from gel phase to sol phase. When activated by calcium, gelsolin can sever assembled actin filaments and can form a cap on the fast-growing end of a free or newly severed filament, thus regulating actin filament length. Moreover, binding of gelsolin to actin causes a conformational change in actin; this can nucleate filament polymerization. Evidence is growing that gelsolin also plays an important role in signal transduction, apoptosis and carcinogenesis.
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