[HTML][HTML] SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei
Signal transducer and activator of transcription (STAT) proteins are both tyrosine-and serine-
phosphorylated, mediating signal transduction and gene regulation. Following gene
regulation, STAT activity in the nucleus is then terminated by a nuclear protein phosphatase
(s), which remains unidentified. Using novel antibody arrays to screen the Stat1-specific
protein phosphatase (s), we identified a SHP-2-Stat1 interaction in the A431 cell nucleus.
SHP-2 and Stat1 nuclear localization and their association in response to either epidermal …
phosphorylated, mediating signal transduction and gene regulation. Following gene
regulation, STAT activity in the nucleus is then terminated by a nuclear protein phosphatase
(s), which remains unidentified. Using novel antibody arrays to screen the Stat1-specific
protein phosphatase (s), we identified a SHP-2-Stat1 interaction in the A431 cell nucleus.
SHP-2 and Stat1 nuclear localization and their association in response to either epidermal …