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J. Biol. Chem., Vol. 265, Issue 11, 6061-6065, Apr, 1990
CJ Fiol, A Wang, RW Roeske and PJ Roach
Recognition of substrates by the protein kinase glycogen synthase kinase 3
(GSK-3) usually requires prior phosphorylation of the substrate. Using a
peptide based on the glycogen synthase sequence PRPAS(3a)VPPS
(3b)PSLS(3c)RHSS(4)PHQS(5)EDEEEP (where the numbers in parentheses denote
sites of phosphorylation), we showed previously that phosphorylation of
site 5 by casein kinase II was necessary for GSK-3 to phosphorylate the
peptide at sites 3a, 3b, 3c, and 4 (Fiol, C. J., Mahrenholz, A. M., Wang,
Y., Roeske, R. W., and Roach, P. J. (1987) J. Biol. Chem. 262,
14042-14048). In the present study, variant peptides were synthesized in
which sites 3a, 3b, 3c, and 4 were individually replaced by Ala residues
(denoted Ala-3c, etc.). All of the variant peptides were substrates for
casein kinase II. The peptide Ala-4,Ser(P)- 5 was not a substrate for GSK-3
confirming the minimal recognition sequence for the protein kinase as
-SXXXS(P)-. The peptides Ala- 3c,Ser(P)-5, Ala-3b,Ser(P)-5, and
Ala-3a,Ser(P)-5, however, were all good substrates for GSK-3 with apparent
Km values in the range 3-6 microns, comparable with that of the parent
peptide. GSK-3 could introduce 1, 2, and 3 phosphates, respectively, into
these substrates, always COOH-terminal to the substituted Ala residue.
Ala-4,Ser(P)-5 and Ala-3c,Ser(P)-4,Ser(P)-5 were competitive inhibitors for
phosphorylation of the parent peptide, with Ki values of 2 and 5 microns,
respectively. The data suggest (i) that GSK-3 recognizes serines in the
motif -SXXXS(P)-, and (ii) that multiple phosphorylation of the peptide
substrate has an obligate order, with the sequential formation of new
recognition sequences.
Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates
Department of Biochemistry, Indiana University School of Medicine, Indianapolis 46223.
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