TY - JOUR
T1 - Polo-like kinase is a cell cycle-regulated kinase activated during mitosis
AU - Hamanaka, Ryoji
AU - Smith, Mark R.
AU - O'Connor, Patrick M.
AU - Maloid, Sharon
AU - Mihalic, Kelly
AU - Spivak, Jerry L.
AU - Longo, Dan L.
AU - Ferris, Douglas K.
PY - 1995/9/8
Y1 - 1995/9/8
N2 - Previously, we demonstrated that expression of polo-like kinase (PLK) is required for cellular DNA synthesis and that overexpression of PLK is sufficient to induce DNA synthesis. We now report that the endogenous levels of PLK, its phosphorylation status, and protein kinase activity are tightly regulated during cell cycle progression. PLK protein is low in G1, accumulates during S and G2M, and is rapidly reduced after mitosis. During mitosis, PLK is phosphorylated on serine, and its serine threonine kinase function is activated at a time close to that of p34(cdc2). The phosphorylated form of PLK migrates with reduced mobility on SDS- polyacrylamide gel electrophoresis, and dephosphorylation by purified protein phosphatase 2A converts it to the more rapidly migrating form and reduces the total amount of PLK kinase activity. Purified p34(cdc2)-cyclin B complex can phosphorylate PLK protein in vitro but causes little increase in PLK kinase activity.
AB - Previously, we demonstrated that expression of polo-like kinase (PLK) is required for cellular DNA synthesis and that overexpression of PLK is sufficient to induce DNA synthesis. We now report that the endogenous levels of PLK, its phosphorylation status, and protein kinase activity are tightly regulated during cell cycle progression. PLK protein is low in G1, accumulates during S and G2M, and is rapidly reduced after mitosis. During mitosis, PLK is phosphorylated on serine, and its serine threonine kinase function is activated at a time close to that of p34(cdc2). The phosphorylated form of PLK migrates with reduced mobility on SDS- polyacrylamide gel electrophoresis, and dephosphorylation by purified protein phosphatase 2A converts it to the more rapidly migrating form and reduces the total amount of PLK kinase activity. Purified p34(cdc2)-cyclin B complex can phosphorylate PLK protein in vitro but causes little increase in PLK kinase activity.
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U2 - 10.1074/jbc.270.36.21086
DO - 10.1074/jbc.270.36.21086
M3 - Article
C2 - 7673138
AN - SCOPUS:0029134127
SN - 0021-9258
VL - 270
SP - 21086
EP - 21091
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -