The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation
The protein-tyrosine phosphatase SHP-1 plays a variety of roles in the" negative" regulation
of cell signaling. The molecular basis for the regulation of SHP-1 is incompletely understood.
Whereas SHP-1 has previously been shown to be phosphorylated on two tail tyrosine
residues (Tyr 536 and Tyr 564) by several protein-tyrosine kinases, the effects of these
phosphorylation events have been difficult to address because of the intrinsic instability of
the linkages within a protein-tyrosine phosphatase. Using expressed protein ligation, we …
of cell signaling. The molecular basis for the regulation of SHP-1 is incompletely understood.
Whereas SHP-1 has previously been shown to be phosphorylated on two tail tyrosine
residues (Tyr 536 and Tyr 564) by several protein-tyrosine kinases, the effects of these
phosphorylation events have been difficult to address because of the intrinsic instability of
the linkages within a protein-tyrosine phosphatase. Using expressed protein ligation, we …