[HTML][HTML] Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase
GG Chiang, BM Sefton - Journal of Biological Chemistry, 2001 - ASBMB
The protein-tyrosine phosphatase SHP-1 has been shown to be a negative regulator of
multiple signaling pathways in hematopoietic cells. In this study, we demonstrate that SHP-1
dephosphorylates the lymphoid-specific Src family kinase Lck at Tyr-394 when both are
transiently co-expressed in nonlymphoid cells. We also demonstrate that a GST-SHP-1
fusion protein specifically dephosphorylates Lck at Tyr-394 in vitro. Because
phosphorylation of Tyr-394 activates Lck, the fact that SHP-1 specifically dephosphorylates …
multiple signaling pathways in hematopoietic cells. In this study, we demonstrate that SHP-1
dephosphorylates the lymphoid-specific Src family kinase Lck at Tyr-394 when both are
transiently co-expressed in nonlymphoid cells. We also demonstrate that a GST-SHP-1
fusion protein specifically dephosphorylates Lck at Tyr-394 in vitro. Because
phosphorylation of Tyr-394 activates Lck, the fact that SHP-1 specifically dephosphorylates …