Calcium/calmodulin‐dependent regulation of the NH2‐terminal F‐actin binding domain of utrophin

FEBS Letters

Kendrick-Jones, J.¹  Winder, S.J.¹ 

[1] MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

关键词: Utrophin;    Dystrophin;    α-Actinin;    Actin binding;    Calcium-calmodulin;    Regulation;   

DOI  :  10.1016/0014-5793(94)01347-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cytoskeletal proteins utrophin, dystrophin and α-actinin are predicted to form antiparallel dimers thus potentially bringing their NH₂-terminal F-actin binding domains in close proximity to their EF-hand containing COOH-terminal domains. This arrangement would allow for calcium-dependent regulation of F-actin binding. We tested this hypothesis by determining the effect of the ubiquitous calcium binding protein calmodulin on their F-actin binding capabilities. Binding of the NH₂-terminal F-actin binding domain of utrophin to F-actin was inhibited by increasing concentrations of calmodulin in a calcium-dependent manner. The homologous F-actin binding domains from dystrophin and α-actinin were not regulated by calmodulin in the presence or absence of calcium. These findings have implications for the structural organisation of utrophin dimers and also for the replacement of dystrophin by over-expression of utrophin in dystrophic muscle.

【 授权许可】

Unknown