TY - JOUR
T1 - Characterization of a novel cdk1-related kinase
AU - Détivaud, Lénaïck
AU - Pettit, George
AU - Meijer, Laurent
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1999/8/15
Y1 - 1999/8/15
N2 - The p13(suc1)/p9(CKShs) proteins bind tightly to the cyclin-dependent kinases cdk1 and cdk2. The distantly related protein, p15(cdk-BP), binds cdk4/6, cdk5 and cdk8. We now show that immobilized p15(cdk-BP) binds both an HMG-I kinase and a 35-kDa protein that cross-reacts with anti-PSTAIRE antibodies (PSTAIRE is a totally conserved motif located in subdomain III of cdk). This 'cdkX' and the HMG-I kinase also bind to an immobilized inhibitor of cdks (HD). Several properties clearly distinguish cdkX, and its associated HMG-I kinase, from known anti-PSTAIRE cross-reactive cdks: (a) cdkX migrates, in SDS/PAGE, in a position intermediate between prophase phosphorylated cdk1 and metaphase dephosphorylated cdk1; (b) in contrast with cdk1, cdkX and associated HMG-I kinase activity do not decrease following successive depletions on p9(CKShs1)-sepharose; (c) cdkX and associated HMG-I kinase activity, but not cdk1, decrease following depletions on immobilized inhibitor; (d) cdkX is expressed during the early development of sea urchin embryos; in contrast with cdk1/cyclin B kinase, the p15(cdk-BP)-bound HMG-I kinase is active throughout the cell cycle; compared with cdk1 it is active later in development; (e) p15(cdk-BP)-bound HMG-I kinase is essentially insensitive to powerful inhibitors of cdk such as purvalanol, roscovitine, olomoucine, p21(cip1) and p16(INK4A); HD is only moderately inhibitory. Altogether these results suggest the existence of a new cdk1-related kinase, possibly involved in the regulation of early development. The presence of this kinase in all organisms investigated so far, from plants to mammals, calls for its definitive identification.
AB - The p13(suc1)/p9(CKShs) proteins bind tightly to the cyclin-dependent kinases cdk1 and cdk2. The distantly related protein, p15(cdk-BP), binds cdk4/6, cdk5 and cdk8. We now show that immobilized p15(cdk-BP) binds both an HMG-I kinase and a 35-kDa protein that cross-reacts with anti-PSTAIRE antibodies (PSTAIRE is a totally conserved motif located in subdomain III of cdk). This 'cdkX' and the HMG-I kinase also bind to an immobilized inhibitor of cdks (HD). Several properties clearly distinguish cdkX, and its associated HMG-I kinase, from known anti-PSTAIRE cross-reactive cdks: (a) cdkX migrates, in SDS/PAGE, in a position intermediate between prophase phosphorylated cdk1 and metaphase dephosphorylated cdk1; (b) in contrast with cdk1, cdkX and associated HMG-I kinase activity do not decrease following successive depletions on p9(CKShs1)-sepharose; (c) cdkX and associated HMG-I kinase activity, but not cdk1, decrease following depletions on immobilized inhibitor; (d) cdkX is expressed during the early development of sea urchin embryos; in contrast with cdk1/cyclin B kinase, the p15(cdk-BP)-bound HMG-I kinase is active throughout the cell cycle; compared with cdk1 it is active later in development; (e) p15(cdk-BP)-bound HMG-I kinase is essentially insensitive to powerful inhibitors of cdk such as purvalanol, roscovitine, olomoucine, p21(cip1) and p16(INK4A); HD is only moderately inhibitory. Altogether these results suggest the existence of a new cdk1-related kinase, possibly involved in the regulation of early development. The presence of this kinase in all organisms investigated so far, from plants to mammals, calls for its definitive identification.
KW - CKS
KW - CKShsl
KW - Cdc2
KW - Cdk-BP
KW - Cell cycle
KW - Cyclin-dependent kinases
KW - HMG-I
KW - PSTAIRE
KW - Suc1
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UR - http://www.scopus.com/inward/citedby.url?scp=0033567322&partnerID=8YFLogxK
U2 - 10.1046/j.1432-1327.1999.00576.x
DO - 10.1046/j.1432-1327.1999.00576.x
M3 - Article
C2 - 10447673
AN - SCOPUS:0033567322
SN - 0014-2956
VL - 264
SP - 55
EP - 66
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 1
ER -