Journal article
Dynamic changes to the skeletal muscle proteome and ubiquitinome induced by the E3 ligase, ASB2β
CA Goodman, JR Davey, A Hagg, BL Parker, P Gregorevic
Molecular and Cellular Proteomics | ELSEVIER | Published : 2021
Abstract
Ubiquitination is a posttranslational protein modification that has been shown to have a range of effects, including regulation of protein function, interaction, localization, and degradation. We have previously shown that the musclespecific ubiquitin E3 ligase, ASB2β, is downregulated in models of muscle growth and that overexpression ASB2β is sufficient to induce muscle atrophy. To gain insight into the effects of increased ASB2β expression on skeletal muscle mass and function, we used liquid chromatography coupled to tandem mass spectrometry to investigate ASB2β-mediated changes to the skeletal muscle proteome and ubiquitinome, via a parallel analysis of remnant diGly-modified peptides. T..
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Grants
Awarded by University of Melbourne
Funding Acknowledgements
Studies were supported by project grants (1121500, 1156562) from the National Health and Medical Research Council of Australia (NHMRC), an Early Career Fellowship (1072129, NHMRC, Australia) and Driving Research Momentum scheme (The University of Melbourne) awarded to B. L. P., and a Senior Research Fellowship (1117835, NHMRC, Australia) awarded to P. G. A. H. was supported by an Australian Post Graduate Award (Department of Education and Training, Australian Government) and a PhD stipend top-up award from the Baker Heart and Diabetes Institute Bright Sparks program.