[HTML][HTML] Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/protein kinase Cμ
SA Matthews, E Rozengurt, D Cantrell - Journal of biological chemistry, 1999 - ASBMB
Activation of the serine kinase protein kinase D (PKD)/PKCμ is controlled by the
phosphorylation of two serine residues within its activation loop via a PKC-dependent
signaling cascade. In this study we have identified the C-terminal serine 916 residue as an
in vivo phosphorylation site within active PKD/PKCμ. An antibody that recognized
PKD/PKCμ proteins specifically phosphorylated on the serine 916 residue was generated
and used to show that phosphorylation of Ser-916 is induced by phorbol ester treatment of …
phosphorylation of two serine residues within its activation loop via a PKC-dependent
signaling cascade. In this study we have identified the C-terminal serine 916 residue as an
in vivo phosphorylation site within active PKD/PKCμ. An antibody that recognized
PKD/PKCμ proteins specifically phosphorylated on the serine 916 residue was generated
and used to show that phosphorylation of Ser-916 is induced by phorbol ester treatment of …