TY - JOUR
T1 - Activation of cdc2 protein kinase during mitosis in human cells
T2 - Cell cycle-dependent phosphorylation and subunit rearrangement
AU - Draetta, Giulio
AU - Beach, David
N1 - Funding Information:
Monika Stein is thanked for technical assistance and Gilbert Morris for advice on HeLa cell elutriation. We acknowledge the assistance of Linda Rodgers with flow cytometry, of Georgia Binns with peptide synthesis, and Jeannie Wiggins with culture of HeLa cells. The artistic assistance of Jim Duffy and Dave Greene is also acknowledged. Bruce Stillman, Paul Young, Maureen McLeod, Robert Booher, and Leonardo Brizuela are thanked for critical comments on the manuscript. This work was supported by National Institutes of Health grant GM34607 to D. B. and a Cold Spring Harbor Robertson Fellowship to G. D.
PY - 1988/7/1
Y1 - 1988/7/1
N2 - HeLa cell p34, homolog of the yeast cdc2+/CDC28 protein kinase, has been investigated. p34 was phosphorylated at two or more sites and existed in a complex with p13, the previously identified homolog of the suc1+ gene product of S. pombe. A fraction of the most highly phosphorylated form of p34 was also associated with p62, a newly identified protein that became phosphorylated in vitro. The phosphorylation state of p34, its association with p62, and the protein kinase activity of the complex were each subject to cell cycle regulation. In newly born cells early in G1, p34 was unphosphorylated, not associated with p62, and inactive as a protein kinase. Each of these conditions was reversed in G2 and the p34/p62 complex was maximally activewas a protein kinase, with respect to both endogenous and exogenous substrates, during mitotic metaphase. p34 may act to regulate the G2/M transition in HeLa cells.
AB - HeLa cell p34, homolog of the yeast cdc2+/CDC28 protein kinase, has been investigated. p34 was phosphorylated at two or more sites and existed in a complex with p13, the previously identified homolog of the suc1+ gene product of S. pombe. A fraction of the most highly phosphorylated form of p34 was also associated with p62, a newly identified protein that became phosphorylated in vitro. The phosphorylation state of p34, its association with p62, and the protein kinase activity of the complex were each subject to cell cycle regulation. In newly born cells early in G1, p34 was unphosphorylated, not associated with p62, and inactive as a protein kinase. Each of these conditions was reversed in G2 and the p34/p62 complex was maximally activewas a protein kinase, with respect to both endogenous and exogenous substrates, during mitotic metaphase. p34 may act to regulate the G2/M transition in HeLa cells.
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U2 - 10.1016/0092-8674(88)90175-4
DO - 10.1016/0092-8674(88)90175-4
M3 - Article
C2 - 3289755
AN - SCOPUS:0023735159
SN - 0092-8674
VL - 54
SP - 17
EP - 26
JO - Cell
JF - Cell
IS - 1
ER -