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Liver proteomics of the HMDP - Hepatosteatosis underlies several diseases including type 2 diabetes, cardiovascular disease and liver disease

ABSTRACT: Hepatosteatosis underlies several diseases including type 2 diabetes, cardiovascular disease and liver disease. Unfortunately, our understanding of the contributing pathways that initiate and advance hepatosteatosis to subsequent complications is still poorly understood. Here, we take advantage of recent developments in “omics” technologies to perform high resolution proteomics (>5000 proteins) and quantitative lipidomics (>300 lipids) on livers from 107 genetically diverse inbred mouse strains from the hybrid mouse diversity panel. Integration of these data allowed us to define novel regulators of lipid metabolism in the liver.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Benjamin Parker

LAB HEAD: Benjamin Parker

PROVIDER: PXD007281 | Pride | 2019-11-01

REPOSITORIES: Pride

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			Action	DRS
	150214_Fusion_BP_HMDP_TMT1_1.raw	Raw
	150214_Fusion_BP_HMDP_TMT1_10.raw	Raw
	150214_Fusion_BP_HMDP_TMT1_11.raw	Raw
	150214_Fusion_BP_HMDP_TMT1_2.raw	Raw
	150214_Fusion_BP_HMDP_TMT1_3.raw	Raw

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Project description:Ubiquitination is a post-translational modification that has been shown to have a range of effects, such as regulating protein function, protein:protein interactions, protein localization, and protein abundance by targeting proteins for degradation by the 26S proteasome. We have previously shown that the muscle-specific ubiquitin E3 ligase, ASB2, is down-regulated in models of muscle growth and that overexpression ASB2 is sufficient to induce muscle atrophy. To gain insight into the effect of increased ASB2 expression on skeletal muscle mass and function, we used 2-dimensional nano-ultra-high-performance mass spectrometry to investigate ASB2-induced changes to the mouse skeletal muscle proteome, and whether these were associated with changes in protein ubiquitination. The results show that in vivo recombinant adeno-associated viral vector-mediated ASB2β overexpression induces impaired intrinsic force production and progressive muscle atrophy over 12 weeks, while ASB2 knockdown induces mild muscle hypertrophy. ASB2-induced muscle atrophy and dysfunction were associated with the early down regulation of mitochondrial and contractile proteins, and the upregulation of proteins involved in proteasome-mediated protein degradation, protein synthesis and the cytoskeleton/sarcomere. The overexpression ASB2β also resulted in marked changes in protein ubiquitination, however, there was no simple relationship between changes in ubiquitination status and protein abundance. To gain insights into proteins that interact with ASB2, and potential ASB2 targets, in muscle cells, flag-tagged wild type ASB2, and a mutant ASB2 with a deleted C-terminal SOCS box domain (dSOCS) were immunoprecipitated from C2C12 myotubes and subjected to label-free proteomic analysis to determine the ASB2 interactome. ASB2β was found to interact with a range of cytoskeletal and nuclear proteins. When combined with the in vivo ubiquitinomic data, we identified several novel potential ASB2β target substrates that await further investigation. Overall, this study reveals for the first time the complexity of changes to the proteome and ubiquitinome during E3 ligase-mediated skeletal muscle atrophy and dysfunction.

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Liver proteomics of the HMDP - Hepatosteatosis underlies several diseases including type 2 diabetes, cardiovascular disease and liver disease

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