Actin bundling via LIM domains

Clément Thomas*, Monika Dieterle, Sabrina Gatti, Céline Hoffmann, Flora Moreau, Jessica Papuga, André Steinmetz

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)


The LIM domain is defined as a protein-protein interaction module involved in the regulation of diverse cellular processes including gene expression and cytoskeleton organization. We have recently shown that the tobacco WLIM1, a two LIM domain-containing protein, is able to bind to, stabilize and bundle actin filaments, suggesting that it participates to the regulation of actin cytoskeleton structure and dynamics. In the December issue of the Journal of Biological Chemistry we report a domain analysis that specifically ascribes the actin-related activities of WLIM1 to its two LIM domains. Results suggest that LIM domains function synergistically in the full-length protein to achieve optimal activities. Here we briefly summarize relevant data regarding the actin-related properties/functions of two LIM domain-containing proteins in plants and animals. In addition, we provide further evidence of cooperative effects between LIM domains by transiently expressing a chimeric multicopy WLIM1 protein in BY2 cells.

Original languageEnglish
Pages (from-to)320-321
Number of pages2
JournalPlant Signaling and Behavior
Issue number5
Publication statusPublished - May 2008


  • Actin-binding proteins
  • Actin-bundling
  • Cysteine-rich proteins
  • Cytoskeleton
  • LIM domain


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