[HTML][HTML] Identification of different specificity requirements between SGK1 and PKBα
NDRG1 is phosphorylated by SGK1 (but not PKB) in vivo at three residues each contained
within three nonapeptide repeats. Here, we demonstrate that this nonapeptide, like the
NDRG1 protein, is phosphorylated by SGK1, but not by PKBα or RSK1 in vitro. The inability
of PKBα and RSK1 to phosphorylate the nonapeptide was traced to residues n+ 1, n+ 2 and
n− 4 (where n is the phosphorylation site). Changing them from Ser, Glu and Ser to Phe, Ala
and Pro, respectively, transformed the nonapeptide into an excellent substrate for PKBα and …
within three nonapeptide repeats. Here, we demonstrate that this nonapeptide, like the
NDRG1 protein, is phosphorylated by SGK1, but not by PKBα or RSK1 in vitro. The inability
of PKBα and RSK1 to phosphorylate the nonapeptide was traced to residues n+ 1, n+ 2 and
n− 4 (where n is the phosphorylation site). Changing them from Ser, Glu and Ser to Phe, Ala
and Pro, respectively, transformed the nonapeptide into an excellent substrate for PKBα and …
NDRG1 is phosphorylated by SGK1 (but not PKB) in vivo at three residues each contained within three nonapeptide repeats. Here, we demonstrate that this nonapeptide, like the NDRG1 protein, is phosphorylated by SGK1, but not by PKBα or RSK1 in vitro. The inability of PKBα and RSK1 to phosphorylate the nonapeptide was traced to residues n+1, n+2 and n−4 (where n is the phosphorylation site). Changing them from Ser, Glu and Ser to Phe, Ala and Pro, respectively, transformed the nonapeptide into an excellent substrate for PKBα and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.
Elsevier