Journal article

Dynamic Changes to the Skeletal Muscle Proteome and Ubiquitinome Induced by the E3 Ligase, ASB2 beta

Craig A Goodman, Jonathan R Davey, Adam Hagg, Benjamin L Parker, Paul Gregorevic

MOLECULAR & CELLULAR PROTEOMICS | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | 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 muscle-specific 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. ..

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Grants

Awarded by National Health and Medical Research Council of Australia (NHMRC)


Awarded by Early Career Fellowship (NHMRC, Australia)


Awarded by Senior Research Fellowship (NHMRC, Australia)


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.