March 15, 1992The Journal of Cell BiologyOpen Access

Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain.

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Population

Monkey Cos cells and E. coli expressing chick smooth muscle alpha-actinin deletion mutants and dystrophin…

Comparison

Expression of alpha-actinin deletion mutants and… vs Wild-type actin-binding domains

Design

Preclinical

Authors

LHLance HemmingsUniversity of Leicester PKPhilip A. KuhlmanUniversity of Leicester DCDavid R. CritchleyUniversity of Leicester

Discussion

Member takes

Implication

Delineates actin-binding homology between alpha-actinin and dystrophin; leaves open mechanistic insights into muscular dystrophy or cardiomyopathy pending human validation.

Structured PICO

Population

Monkey Cos cells and E. coli expressing chick smooth muscle alpha-actinin deletion mutants and dystrophin fusion proteins

Intervention

Expression of alpha-actinin deletion mutants and dystrophin chimeric proteins

Comparator

Wild-type actin-binding domains

Outcome

Localization to actin filaments/filament ends in Cos cells and binding to F-actin in vitrosurrogate

This basic science study maps the actin-binding domain of alpha-actinin to residues 108-189 and demonstrates that the NH2-terminal domain of dystrophin is functionally homologous.

Cite This Study

Hemmings et al. (1992) studied this question.

synapsesocial.com/papers/6a7256d6a7fbea1e4408a5a0 https://doi.org/10.1083/jcb.116.6.1369

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Implication

Delineates actin-binding homology between alpha-actinin and dystrophin; leaves open mechanistic insights into muscular dystrophy or cardiomyopathy pending human validation.