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Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):11884-9. doi: 10.1073/pnas.1105703108. Epub 2011 Jul 5.

Structure and function of the interacting domains of Spire and Fmn-family formins.

Author information

1
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.

Abstract

Evidence for cooperation between actin nucleators is growing. The WH2-containing nucleator Spire and the formin Cappuccino interact directly, and both are essential for assembly of an actin mesh during Drosophila oogenesis. Their interaction requires the kinase noncatalytic C-lobe domain (KIND) domain of Spire and the C-terminal tail of the formin. Here we describe the crystal structure of the KIND domain of human Spir1 alone and in complex with the tail of Fmn2, a mammalian ortholog of Cappuccino. The KIND domain is structurally similar to the C-lobe of protein kinases. The Fmn2 tail is coordinated in an acidic cleft at the base of the domain that appears to have evolved via deletion of a helix from the canonical kinase fold. Our functional analysis of Cappuccino reveals an unexpected requirement for its tail in actin assembly. In addition, we find that the KIND/tail interaction blocks nucleation by Cappuccino and promotes its displacement from filament barbed ends providing insight into possible modes of cooperation between Spire and Cappuccino.

PMID:
21730168
PMCID:
PMC3141961
DOI:
10.1073/pnas.1105703108
[Indexed for MEDLINE]
Free PMC Article

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