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Identification of Shp-2 as a Stat5A phosphatase. J Biol Chem 2003 May 09;278(19):16520-7



Pubmed ID




Scopus ID

2-s2.0-0037593839   90 Citations


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.

Author List

Chen Y, Wen R, Yang S, Schuman J, Zhang EE, Yi T, Feng GS, Wang D


Demin Wang PhD Assistant Professor in the Microbiology and Immunology department at Medical College of Wisconsin
Renren Wen PhD Associate Investigator in the Blood Research Institute department at BloodCenter of Wisconsin

MESH terms used to index this publication - Major topics in bold

COS Cells
DNA-Binding Proteins
Intracellular Signaling Peptides and Proteins
Milk Proteins
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatases
SH2 Domain-Containing Protein Tyrosine Phosphatases
STAT5 Transcription Factor
Substrate Specificity
src Homology Domains
jenkins-FCD Prod-469 c3fc8ab87196149f9b23743c01b947d47e7319e5