Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase.
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 this site suggests that SHP-1 is a negative regulator of Lck. The failure of SHP-1 to inactivate Lck may contribute to some of the lymphoid abnormalities observed in motheaten mice.
Mesh Terms:
Catalytic Domain, Cell Line, Humans, Intracellular Signaling Peptides and Proteins, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Phosphorylation, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, Tyrosine
Catalytic Domain, Cell Line, Humans, Intracellular Signaling Peptides and Proteins, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Phosphorylation, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, Tyrosine
J. Biol. Chem.
Date: Jun. 22, 2001
PubMed ID: 11294838
View in: Pubmed Google Scholar
Download Curated Data For This Publication
4987
Switch View:
- Interactions 1