TY - JOUR
T1 - Identification of different specificity requirements between SGK1 and PKBα
AU - Murray, James T.
AU - Cummings, Lorna A.
AU - Bloomberg, Graham B.
AU - Cohen, Philip
PY - 2005/2/14
Y1 - 2005/2/14
N2 - 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.
AB - 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.
KW - NDRG1
KW - PKB
KW - Protein kinase specificity
KW - SGK
UR - http://www.scopus.com/inward/record.url?scp=13844280121&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2004.12.069
DO - 10.1016/j.febslet.2004.12.069
M3 - Article
C2 - 15710380
AN - SCOPUS:13844280121
VL - 579
SP - 991
EP - 994
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 5
ER -