期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 278, 期 19, 页码 16520-16527出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M210572200
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资金
- NCI NIH HHS [R01 CA78606, 1R01CA79891] Funding Source: Medline
- NHLBI NIH HHS [R01 HL073284] Funding Source: Medline
- NIAID NIH HHS [R01 AI52327-01] Funding Source: Medline
- NIGMS NIH HHS [R01GM53660, 1R01GM58893] Funding Source: Medline
Stat5A, a member of the signal transducers and activators of transcription (Stat) family, is activated upon a single tyrosine phosphorylation. Although much is known about the activation process, the mechanism by which the tyrosine-phosphorylated Stat5A proteins are inactivated is largely unknown. In this report, we demonstrate that down-regulation of the tyrosine-phosphorylated Stat5A was via dephosphorylation. Using tyrosine-phosphorylated peptides derived from Stat5A, we were able to purify protein-tyrosine phosphatase Shp-2 from cell lysates. Shp-2, but not Shp-1, specifically interacted with Stat5A in vivo, and the interaction was tyrosine phosphorylation-dependent. Moreover, Shp-2 was able to accelerate Stat5A dephosphorylation, and dephosphorylation of Stat5A was dramatically delayed in Shp-2-deficient cells. Therefore, we conclude that Shp-2 is a Stat5A phosphatase, which down-regulates the active Stat5A in vivo.
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