Dataset Information

Redox Proteome of Skeletal Muscle

ABSTRACT: Adult and aged mouse gastrocnemius muscle analysed by redox shotgun proteomics, applying a label free quantitative proteomic approach that includes a differential Cysteine labelling step allowing simultaneous identification of up and down regulated proteins between samples and also the identification and relative quantification of the reversible oxidation state of susceptible redox Cysteine residues.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle Cell, Gastrocnemius

SUBMITTER: Brian McDonagh

LAB HEAD: Brian McDonagh

PROVIDER: PXD001054 | Pride | 2014-09-04

REPOSITORIES: Pride

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Publications

Differential cysteine labeling and global label-free proteomics reveals an altered metabolic state in skeletal muscle aging.

McDonagh Brian B Sakellariou Giorgos K GK Smith Neil T NT Brownridge Philip P Jackson Malcolm J MJ

Journal of proteome research 20140916 11

The molecular mechanisms underlying skeletal muscle aging and associated sarcopenia have been linked to an altered oxidative status of redox-sensitive proteins. Reactive oxygen and reactive nitrogen species (ROS/RNS) generated by contracting skeletal muscle are necessary for optimal protein function, signaling, and adaptation. To investigate the redox proteome of aging gastrocnemius muscles from adult and old male mice, we developed a label-free quantitative proteomic approach that includes a di ...[more]

PMID: 25181601

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Project description:E3 ubiquitin ligases mediate the last step of the ubiquitination pathwayin the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology. In plants, SKP1/CULLIN1/F-BOX PROTEIN (SCF)-type E3 ubiquitin ligases are essential for the perception and signaling of several key hormones including auxins and jasmonates (JAs). F-box proteins, TRANSPORT INHIBITOR RESPONSE 1 (TIR1) and CORONATINE INSENSITIVE 1 (COI1) bind directly transcriptional repressors AUX/IAAs and JAZs in an auxin- and JAs-depending manner, respectively, which permits the perception of the hormones and transcriptional activation of signaling pathways. Redox modification of proteins mainly by S-nitrosation of cysteines via nitric oxide (NO) has emerged as a valued regulatory mechanism in physiological processes requiring its rapid and versatile integration. Previously, we demonstrated that TIR1 and ASK1 (Arabidopsis thaliana SKP1) are targets of S-nitrosation, and these (NO)-dependent post-translational modifications enhance protein-protein interactions, and positively regulate SCFTIR1 complex assembly and expression of auxin response genes. In this work, we provide evidence on the modulation of SCFCOI1 complex by different S-nitrosation events. We demonstrated that S-nitrosation of ASK1 Cys118 enhanced ASK1-COI1 protein-protein interaction. Overexpression of non-nitrosable ask1 mutant protein impaired the activation of JA-responsive genes mediated by SCFCOI1 illustrating the functional relevance of this redox-mediated regulation in planta. Additionally, in silico analysis positioned COI1 as a promising S-nitrosation target. The regulation of SCF components involved in hormonal perception by S- nitrosation may represent a key strategy to determine the precise time and site-dependent activation of each hormonal signaling pathway, and highlights NO as a pivotal molecular player in these scenarios.

Dataset Information

Redox Proteome of Skeletal Muscle

Publications

Differential cysteine labeling and global label-free proteomics reveals an altered metabolic state in skeletal muscle aging.

Similar Datasets

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