[HTML][HTML] B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1
H Zhang, X Shi, H Paddon, M Hampong, W Dai… - Journal of Biological …, 2004 - ASBMB
Phosphoprotein profiling by Kinetworks™ analysis of M-phase-arrested HeLa cells by
nocodazole treatment revealed that a novel mitosis-specific phosphorylation event occurred
in the nucleolar protein B23/nucleophosmin at a conserved Ser-4 residue. Consistent with
the resemblance of the Ser-4 phosphorylation site to the Polo-like kinase 1 (Plk1) consensus
recognition sequence, inhibition of Plk1 by a kinase-defective mutation (K82M) abrogated
B23 Ser-4 phosphorylation, whereas activation of Plk1 by a constitutively active mutation …
nocodazole treatment revealed that a novel mitosis-specific phosphorylation event occurred
in the nucleolar protein B23/nucleophosmin at a conserved Ser-4 residue. Consistent with
the resemblance of the Ser-4 phosphorylation site to the Polo-like kinase 1 (Plk1) consensus
recognition sequence, inhibition of Plk1 by a kinase-defective mutation (K82M) abrogated
B23 Ser-4 phosphorylation, whereas activation of Plk1 by a constitutively active mutation …