Journal article
Phosphorylation of ERK and dystrophin S3059 protects against inflammationassociated C2C12 myotube atrophy
K Swiderski, CJ Brock, J Trieu, A Chee, SS Thakur, DM Baum, P Gregorevic, KT Murphy, GS Lynch
American Journal of Physiology Cell Physiology | Published : 2021
Abstract
The dystrophin-glycoprotein complex (DGC) is a multiprotein structure required to maintain muscle fiber membrane integrity, transmit force by linking the actin cytoskeleton with the extracellular matrix, and maintain muscle homeostasis. Membrane localization of dystrophin is perturbed in muscles wasting as a consequence of cancer cachexia, tenotomy, and advanced aging, which are all associated with low level, chronic inflammation. Strategies to preserve dystrophin expression at the sarcolemma might therefore combat muscle wasting. Phosphorylation of dystrophin serine 3059 (S3059) enhances the interaction between dystrophin and b-dystroglycan. To test the contribution of amino acid phosphoryl..
View full abstractRelated Projects (2)
Grants
Awarded by National Health and Medical Research Council
Funding Acknowledgements
This work was supported by research grants from the National Health and Medical Research Council of Australia (NHMRC) Grants GNT1041865 and GNT1144772. K. Swiderski was supported by an Early Career Fellowship from the NHMRC and an Early Career Seed grant from The University of Melbourne. K. T. Murphy was supported by a Career Development Fellowship from the NHMRC. P. Gregorevic was supported by a Senior Research Fellowship from the NHMRC.