[HTML][HTML] Phosphatidylinositol phosphate kinase type Iγ directly associates with and regulates Shp-1 tyrosine phosphatase
SF Bairstow, K Ling, RA Anderson - Journal of Biological Chemistry, 2005 - ASBMB
Tyrosine phosphorylation plays a critical role in many regulatory aspects of cellular
signaling, and dephosphorylation of phosphotyrosine residues is crucial for termination of
signals initiated by tyrosine kinases. Previous work has shown that the tyrosine kinase Src
phosphorylates Tyr 644 on phosphatidylinositol phosphate kinase type I (PIPKI) γ661 in a
focal adhesion kinase-dependent manner. Phosphorylation of this residue is essential for
high affinity binding of PIPKIγ661 to the focal adhesion protein talin and for targeting of …
signaling, and dephosphorylation of phosphotyrosine residues is crucial for termination of
signals initiated by tyrosine kinases. Previous work has shown that the tyrosine kinase Src
phosphorylates Tyr 644 on phosphatidylinositol phosphate kinase type I (PIPKI) γ661 in a
focal adhesion kinase-dependent manner. Phosphorylation of this residue is essential for
high affinity binding of PIPKIγ661 to the focal adhesion protein talin and for targeting of …
