Proteomics

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Identification of the intermolecular disulfide bonds between NPGPx and ZAP70

ABSTRACT: The tyrosine kinase, ζ-chain-associated protein of 70 kDa (ZAP70), is essential for T cell development and activation. However, it remains elusive whether a direct redox regulation affects ZAP70 activity upon TCR stimulation. Here, we showed that deficiency of non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx), a redox sensor, resulted in T cell hyperproliferation and elevated cytokine productions. Through proteomic approaches, ZAP70 is identified as the key interacting protein of NPGPx through disulfide bonding. Here we utilized the MS/MS spectra to identify the cysteine residues in ZAP70 for NPGPx-mediated regulation. Combined molecular approaches, our results elucidate a delicate redox mechanism that NPGPx serves as a modulator to curb ZAP70 functions in maintaining T cell homeostasis.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Pang-Hung Hsu  

LAB HEAD: Pang-Hung Hsu

PROVIDER: PXD017034 | Pride | 2021-01-25

REPOSITORIES: Pride

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Action DRS
20161029_FangYi-SS_ID.xlsx Xlsx
20161029_Zap70-NPGPx_1.mgf Mgf
20161029_Zap70-NPGPx_1.raw Raw
20161029_Zap70-NPGPx_2.mgf Mgf
20161029_Zap70-NPGPx_2.raw Raw
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Publications

Emerging evidences implicate the contribution of ROS to T cell activation and signaling. The tyrosine kinase, ζ-chain-associated protein of 70 kDa (ZAP70), is essential for T cell development and activation. However, it remains elusive whether a direct redox regulation affects ZAP70 activity upon TCR stimulation. Here, we show that deficiency of non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx), a redox sensor, results in T cell hyperproliferation and elevat  ...[more]

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