Signal transduction
The CEP5 Peptide Promotes Abiotic Stress Tolerance, As Revealed by Quantitative Proteomics, and Attenuates the AUX/IAA Equilibrium in ArabidopsisThe proteome and phosphoproteome of CEP5 overexpressing Arabidopsis seedlings have been determined. This revealed that CEP5 impacts abiotic stress-related processes. Subsequent genetic, physiological, biochemical, and pharmacological results demonstrated that CEP5-mediated signaling is relevant for osmotic and drought stress tolerance in Arabidopsis. Furthermore, CEP5 specifically counteracts auxin effects by stabilizing AUX/IAA transcriptional repressors.
Proteome and Phosphoproteome Analysis of Brown Adipocytes Reveals That RICTOR Loss Dampens Global Insulin/AKT SignalingWe applied DDA proteomics along with DDA and PRM phosphoproteomics to study brown adipocytes lacking RICTOR, an essential subunit of mTOR complex 2, over a time series of insulin stimulation. RICTOR loss caused many protein abundance changes, including increased levels of interferon response proteins. The insulin phosphoproteome response in RICTOR-deficient cells was dampened, including known functional sites ACLY S455, VIM S39, and EIF4B S422, potentially helping to bridge the gap between the acute and chronic effects of RICTOR loss.
Characterization of Signaling Pathways Associated with Pancreatic β-cell Adaptive Flexibility in Compensation of Obesity-linked Diabetes in db/db MiceAn unbiased quantitative profiling of the protein expression, phosphorylation, and sialylation events that occur upon β-cell adaptive flexibility during the transition from hyperglycemia to euglycemia was assessed in islets from db/db and WT mice before and after β-cell rest. Our PTMomics data revealed new adaptive proteins, phosphosites, and SA N-linked glycosites involved in the regulation of proinsulin biosynthesis translation, protein folding, not ER stress, proinsulin processing, β-granule biogenesis, vesicular trafficking and the insulin secretory pathway, protein degradation, and endopeptidase activity, associated with β-cell adaptive flexibility.
NOTCH Activation Promotes Valve Formation by Regulating the Endocardial SecretomeThe NOTCH-dependent endocardial secretome has been determined by quantitative MS-based proteomics of mouse embryonic endocardial cells (MEEC). DLL4-mediated NOTCH activation lead to expression of EMT, cytoskeleton and cell-cell/cell-matrix proteins, whereas JAG1-NOTCH signaling activated ECM molecules expression. Data validation in vitro and in vivo support the value of MEEC as a model for studying the endocardial secretome and for the identification of novel factors potentially involved in heart development and disease.