The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins

Adeleke H. Aguda, Bo Xue, Edward Irobi, Thomas Préat, Robert C. Robinson

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/β-thymosin (βT) domain. WH2/βT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/βT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the βT and WH2 motifs are not functionally analogous.

Original languageEnglish
Pages (from-to)469-476
Number of pages8
JournalStructure
Volume14
Issue number3
DOIs
Publication statusPublished - Mar 2006
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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