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Immunoprecipitated PTPN22 Phosphoproteomics from Jurkat Cells

ABSTRACT: 3x FLAG tagged PTPN22 were immunoprecipitated from Jurkat cells stimulated by TCR for 5min, and the proteins were eluted by FLAG peptides. This study aims to explore the phosphorylation sites on PTPN22 phosphatase, identifying two phosphorylation sites Ser325 and Ser449.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Nunzio Bottini David J Gonzalez

PROVIDER: MSV000093717 | MassIVE | Thu Dec 21 18:24:00 GMT 2023

SECONDARY ACCESSION(S): PXD048062

REPOSITORIES: MassIVE

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Publications

A novel gain-of-function phosphorylation site modulates PTPN22 inhibition of TCR signaling.

Zhuang Chuling C Yang Shen S Gonzalez Carlos G CG Ainsworth Richard I RI Li Sheng S Kobayashi Masumi Takayama MT Wierzbicki Igor I Rossitto Leigh-Ana M LM Wen Yutao Y Peti Wolfgang W Stanford Stephanie M SM Gonzalez David J DJ Murali Ramachandran R Santelli Eugenio E Bottini Nunzio N

The Journal of biological chemistry 20240521 6

Protein tyrosine phosphatase nonreceptor type 22 (PTPN22) is encoded by a major autoimmunity gene and is a known inhibitor of T cell receptor (TCR) signaling and drug target for cancer immunotherapy. However, little is known about PTPN22 posttranslational regulation. Here, we characterize a phosphorylation site at Ser<sup>325</sup> situated C terminal to the catalytic domain of PTPN22 and its roles in altering protein function. In human T cells, Ser<sup>325</sup> is phosphorylated by glycogen sy ...[more]

PMID: 38777143

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