Proteomics

Dataset Information

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DUSP2 dephosphorylates STAT3 at Y705 and S727 residues

ABSTRACT: In the related study, to determine whether DUSP2 definitively served as a phosphatase for STAT3, an in vitro phosphatase assay was used. Using S-tag beads, p-STAT3 was pulled down from IL-6 stimulated HEK293T cells transfected with STAT3-S-Tag. DUSP2 or control protein, which was purified from HEK293T cells transfected with DUSP2-FLAG or empty vector through extraction with anti-FLAG beads and elution with FLAG peptides, were incubated with p-STAT3-S-Tag-beads in phosphatase buffer. Then bound proteins were eluted and subjected to MS analysis. When compared with the control, incubation of STAT3 and DUSP2 led to dephosphorylation of two STAT3 residues that have been reported to promote its activity, namely tyrosine 705 and serine 727.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Dan Lu  

LAB HEAD: Yuxin Yin

PROVIDER: PXD002743 | Pride | 2015-10-13

REPOSITORIES: Pride

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Publications

The phosphatase DUSP2 controls the activity of the transcription activator STAT3 and regulates TH17 differentiation.

Lu Dan D   Liu Liang L   Ji Xin X   Gao Yanan Y   Chen Xi X   Liu Yu Y   Liu Yang Y   Zhao Xuyang X   Li Yan Y   Li Yunqiao Y   Jin Yan Y   Zhang Yu Y   McNutt Michael A MA   Yin Yuxin Y  

Nature immunology 20151019 12

Deregulation of the TH17 subset of helper T cells is closely linked with immunological disorders and inflammatory diseases. However, the mechanism by which TH17 cells are regulated remains elusive. Here we found that the phosphatase DUSP2 (PAC1) negatively regulated the development of TH17 cells. DUSP2 was directly associated with the signal transducer and transcription activator STAT3 and attenuated its activity through dephosphorylation of STAT3 at Tyr705 and Ser727. DUSP2-deficient mice exhib  ...[more]