About the Dystrophin Interactome Project
Background:
Dystrophin has a well understood role in protecting muscle cell membranes from contraction-induced tearing. Other roles include the organization of the microtubule network, regulation of muscle blood perfusion, lipid binding and vesicle trafficking. Many binding domains of dystrophin have already been identified and implicated in pathologies. Despite the significance of dystrophin's interactions, a systematic review of dystrophin's interactome has yet to be carried out.
Dystrophin has a well understood role in protecting muscle cell membranes from contraction-induced tearing. Other roles include the organization of the microtubule network, regulation of muscle blood perfusion, lipid binding and vesicle trafficking. Many binding domains of dystrophin have already been identified and implicated in pathologies. Despite the significance of dystrophin's interactions, a systematic review of dystrophin's interactome has yet to be carried out.
Methods:
We have utilised previously published literature and online interaction databases in combination with our own experimental data to generate a comprehensive interactome of dystrophin. Experimental data was be obtained using the 'QUICK' method for protein interaction screening by quantitative immunoprecipitation combined with knockdown (Selbach, 2008) upon stably immortalised human-derived myoblast cell lines.
We have utilised previously published literature and online interaction databases in combination with our own experimental data to generate a comprehensive interactome of dystrophin. Experimental data was be obtained using the 'QUICK' method for protein interaction screening by quantitative immunoprecipitation combined with knockdown (Selbach, 2008) upon stably immortalised human-derived myoblast cell lines.
Results:
The generation and analysis of the mass spectrometery data has suggested a number of dystrophin direct binding partners in skeletal muscle. Our experimental data and literature data have been used in the tool to expand the interactome to encorporate these possible interactions. Please note that the experimental findings are provided as is, without additional validation.
The generation and analysis of the mass spectrometery data has suggested a number of dystrophin direct binding partners in skeletal muscle. Our experimental data and literature data have been used in the tool to expand the interactome to encorporate these possible interactions. Please note that the experimental findings are provided as is, without additional validation.
Acknowledgements:
This work was supported by the Association Française contre les Myopathies (AFM), the MyoGrad doctoral training scheme, and the Duchenne Parent Project (Netherlands).
This work was supported by the Association Française contre les Myopathies (AFM), the MyoGrad doctoral training scheme, and the Duchenne Parent Project (Netherlands).
