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Int J Biochem Cell Biol. 2008;40(9):1806-16. doi: 10.1016/j.biocel.2008.01.011. Epub 2008 Jan 19.

Synthetic actin-binding domains reveal compositional constraints for function.

Author information

1
Consorzio Mario Negri Sud, Department of Cell Biology and Oncology, Via Nazionale 8a, I-66030 Santa Maria Imbaro, Italy.

Abstract

The actin-binding domains of many proteins consist of a canonical type 1/type 2 arrangement of the structurally conserved calponin homology domain. Using the actin-binding domain of alpha-actinin-1 as a scaffold we have generated synthetic actin-binding domains by altering position and composition of the calponin homology domains. We show that the presence of two calponin homology domains alone and in the context of an actin-binding domain is not sufficient for actin-binding, and that both single and homotypic type 2 calponin homology domain tandems fail to bind to actin in vitro and in transfected cells. In contrast, single and tandem type 1 calponin homology domain arrays bind actin directly but result in defective turnover rates on actin filaments, and in aberrant actin bundling when introduced into the full-length alpha-actinin molecule. An actin-binding domain harboring the calponin homology domains in an inverted position, however, functions both in isolation and in the context of the dimeric alpha-actinin molecule. Our data demonstrate that the dynamics and specificity of actin-binding via actin-binding domains requires both the filament binding properties of the type 1, and regulation by type 2 calponin homology domains, and appear independent of their position.

PMID:
18296101
DOI:
10.1016/j.biocel.2008.01.011
[Indexed for MEDLINE]

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