TY - JOUR
T1 - The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins
AU - Aguda, Adeleke H.
AU - Xue, Bo
AU - Irobi, Edward
AU - Préat, Thomas
AU - Robinson, Robert C.
N1 - Funding Information:
We are grateful to the MAX-Lab, Lund and ESRF, Grenoble for the provision of synchrotron radiation facilities. We thank the Swedish Medical Science Research Council; the Wenner-Gren Foundation, Sweden (B.X.); and A ∗ STAR, Singapore for their financial support. This work is supported by the Swedish Research Council and by A ∗ STAR. The authors declare that they have no competing financial interests.
PY - 2006/3
Y1 - 2006/3
N2 - 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.
AB - 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.
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U2 - 10.1016/j.str.2005.12.011
DO - 10.1016/j.str.2005.12.011
M3 - Article
C2 - 16531231
AN - SCOPUS:33644835262
SN - 0969-2126
VL - 14
SP - 469
EP - 476
JO - Structure with Folding & design
JF - Structure with Folding & design
IS - 3
ER -