What question did this study set out to answer?

To investigate the molecular binding and cross-linking characteristics of the native skeletal muscle dystrophin-glycoprotein complex with filamentous actin.

November 1, 1996The Journal of Cell BiologyOpen Access

A new model for the interaction of dystrophin with F-actin.

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Authors

IRInna N. RybakovaUniversity of Wisconsin–Madison KAKurt J. AmannUniversity of Wisconsin–Madison JEJames M. ErvastiUniversity of Iowa

Discussion

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Implication

May inform cytoskeletal mechanisms in dystrophin-related cardiomyopathy; leaves open therapeutic targeting in cardiac muscle.

Key Points

To investigate the molecular binding and cross-linking characteristics of the native skeletal muscle dystrophin-glycoprotein complex with filamentous actin.
Evaluated native dystrophin-glycoprotein complex binding and cross-linking to F-actin using high- and low-speed cosedimentation assays, microcapillary falling ball viscometry, and electron microscopy, with alpha-actinin as a positive control.
Mapped actin-binding domains by analyzing calpain-digested dystrophin-glycoprotein complex and recombinant dystrophin fragments including the first 246 amino acids and a central rod domain region.
Dystrophin-glycoprotein complex bound F-actin with an apparent dissociation constant (Kd) of 0.5 µM and saturated near 0.042 ± 0.005 mol/mol (1 dystrophin per 24 actin monomers), but showed no cross-linking activity across three distinct assays.
High-speed cosedimentation of calpain-cleaved complex identified a novel F-actin binding site in the middle of the rod domain, with recombinant fragments displaying lower affinity and higher capacity than the intact complex.
The native complex significantly slowed F-actin depolymerization, indicating dystrophin aligns along the filament surface across multiple actin monomers.

Cite This Study

Rybakova et al. (1996) studied this question.

synapsesocial.com/papers/6a85a6596f8d490ba41e72b7 https://doi.org/10.1083/jcb.135.3.661

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A new model for the interaction of dystrophin with F-actin.

Discussion

Member takes

Implication

Key Points

Cite This Study

A new model for the interaction of dystrophin with F-actin.

Discussion

Member takes

Implication

Key Points

Cite This Study

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