Proteomics

Dataset Information

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In-vitro glutathionylation of SMYD2

ABSTRACT: Glutathionylation is an important post-translational modification and developing tools to identify which cysteine residues on proteins are glutathionylated in response to different physiological conditions is necessary. This project utilizes an approach consisting of azido-glutathione, a single purified protein, and an oxidant to form disulfide bonds between the azide modified glutathione and the cysteine residues of the protein. After this the reaction is quenched with iodoacetamide, subjected to a click reaction with a chemically cleavable alkyne conjugated biotin, and digested with trypsin. These peptide fragments are eluted from streptavidin beads and subjected to LC-MS/MS to determine which cysteine residues are glutathionylated in-vitro.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: garrett vanhecke  

LAB HEAD: Young-Hoon Ahn

PROVIDER: PXD011123 | Pride | 2019-04-03

REPOSITORIES: Pride

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Dataset's files

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Action DRS
1984-Ahn-131c.mzid.gz Mzid
1984-Ahn-131c.mzid_1984-Ahn-131c.MGF Mzid
1984-Ahn-131c.mzid_1984-Ahn-131c.pride.mgf.gz Mzid
1984-Ahn-131c.pride.mztab.gz Mztab
1984-Ahn-131c.raw Raw
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Publications

Reactive oxygen species (ROS) contribute to the etiology of multiple muscle-related diseases. There is emerging evidence that cellular stress can lead to destabilization of sarcomeres, the contractile unit of muscle. However, it is incompletely understood how cellular stress induces structural destabilization of sarcomeres. Here we report that glutathionylation of SMYD2 contributes to a loss of myofibril integrity and degradation of sarcomeric proteins mediated by MMP-2 and calpain 1. We used a  ...[more]

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