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Calcium/calmodulin‐dependent regulation of the NH 2 ‐terminal F‐actin binding domain of utrophin
Author(s) -
Winder S.J.,
Kendrick-Jones J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01347-4
Subject(s) - utrophin , calmodulin , dystrophin , actin , calcium , microbiology and biotechnology , ef hand , cytoskeleton , actinin , chemistry , biophysics , binding protein , binding domain , plasma protein binding , calcium binding protein , actin binding protein , biochemistry , binding site , actin cytoskeleton , biology , cell , organic chemistry , gene
The cytoskeletal proteins utrophin, dystrophin and α‐actinin are predicted to form antiparallel dimers thus potentially bringing their NH 2 ‐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 NH 2 ‐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.