The gelsolin:calponin complex nucleates actin filaments with distinct morphologies

Imen Ferjani, Abdellatif Fattoum, Nadir Bettache, Bastien Seantier, Pierre-Emmanuel Milhiet, Mohamed Manai, Yves Benyamin, Claude Roustan, Sutherland K. Maciver

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Gelsolin and calponin are cytoskeletal and signalling proteins that form a tight 1:1 complex (GCC). We show that calponin within the GCC inhibits the rate of gelsolin mediated nucleation of actin polymerization. The actin-binding function of calponin is ablated within the GCC as the actin-binding site overlaps with one of the gelsolin binding sites. The structure of filaments that result from nucleation by GCC are different to those nucleated by gelsolin alone in that they are longer, loosely bundled and stain heterogeneously with phalloidin. GCC nucleated filaments appear contorted and wrap around each to form the loose bundles. (C) 2009 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)118-123
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 5 Feb 2010


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