Troponin T is capable of binding dystrophin via a leucine zipper

FEBS Letters

Powaser, Peter A.¹  Pearlman, Joel A.¹  Elledge, Stephen J.²  Caskey, C.Thomas¹ 

[1] Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030, USA;Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA

关键词: Duchenne muscular dystrophy;    Dystrophin;    Troponin;    Protein—protein interaction;    Cytoskeleton;   

DOI  :  10.1016/0014-5793(94)01119-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using genetic and physical assays for protein—protein interactions, we identified a fast isoform of troponin T that binds to dystrophin. Troponin T specifically bound to the first of two highly conserved leucine zipper motifs in the carboxy terminus of dystrophin [1,2]. Single amino acid changes in the zipper predicted to disrupt α-helix formation or cause steric hindrance abolished this binding. These data support the hypothesis that dystrophin couples the contractile apparatus to the sarcolemma and indicate that leucine zipper mediated protein—protein interactions are functionally important in the cytoskeleton as well as the nucleus.

【 授权许可】

Unknown