부산대학교 도서관

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.str.2005.12.011 Byline: Adeleke H. Aguda (1)(2), Bo Xue (1)(2), Edward Irobi (1), Thomas Preat (3), Robert C. Robinson (1)(2) Keywords: CELLBIO 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)/[beta]-thymosin ([beta]T) domain. WH2/[beta]T 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/[beta]T 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 [beta]T and WH2 motifs are not functionally analogous. Author Affiliation: (1) Department of Medical Biochemistry and Microbiology, Uppsala Biomedical Center, Uppsala University, Uppsala 751 23, Sweden (2) Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore (3) Institut de Neurobiologie Alfred Fessard, CNRS, 91190 Gif-sur-Yvette, France Article History: Received 4 March 2005; Revised 15 November 2005; Accepted 15 December 2005 Article Note: (miscellaneous) Published online: March 14, 2006