Gelsolin superfamily proteins: Key regulators of cellular functions

P. Silacci, L. Mazzolai, C. Gauci, N. Stergiopulos, H. L. Yin, D. Hayoz

Research output: Contribution to journalReview articlepeer-review

319 Scopus citations


Cytoskeletal rearrangement occurs in a variety of cellular processes and involves a wide spectrum of proteins. Among these, the gelsolin superfamily proteins control actin organization by severing filaments, capping filament ends and nucleating actin assembly [1]. Gelsolin is the founding member of this family, which now contains at least another six members: villin, adseverin, capG, advillin, supervillin and flightless I. In addition to their respective role in actin filament remodeling, these proteins have some specific and apparently non-overlapping particular roles in several cellular processes, including cell motility, control of apoptosis and regulation of phagocytosis (summarized in table 1). Evidence suggests that proteins belonging to the gelsolin superfamily may be involved in other processes, including gene expression regulation. This review will focus on some of the known functions of the gelsolin superfamily proteins, thus providing a basis for reflection on other possible and as yet incompletely understood roles for these proteins.

Original languageEnglish (US)
Pages (from-to)2614-2623
Number of pages10
JournalCellular and Molecular Life Sciences
Issue number19-20
StatePublished - Oct 2004


  • Actin network
  • Apoptosis
  • Cytoskeleton
  • Gelsolin
  • Gelsolin superfamily
  • Phagocytosis

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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