PMID- 10653604
OWN - NLM
STAT- MEDLINE
DCOM- 20000210
LR  - 20151119
IS  - 0021-9541 (Print)
IS  - 0021-9541 (Linking)
VI  - 182
IP  - 3
DP  - 2000 Mar
TI  - Posttranslational modifications of the KI-67 protein coincide with two major
      checkpoints during mitosis.
PG  - 371-80
AB  - Ki-67 is a nuclear protein present in all proliferating cells that are in the
      active part of the cell division, but not in resting cells. This feature is
      extensively used in tumor diagnostics to estimate the growth fraction of a given 
      cell population. We now demonstrate that the spatial and temporal regulation of
      the Ki-67 protein during the cell cycle is associated with mitosis-specific
      phosphorylation. These posttranslational modifications of the Ki-67 protein are
      accompanied by a characteristic redistribution of the protein from the interior
      of the nucleus to the periphery of the condensed chromosomes and vice versa.
      Phosphorylation could be suppressed by activating cell-cycle checkpoints that
      control the entry into mitosis through the activity of the cyclin B/cdc2 complex.
      In vitro experiments confirm that the presence of the cdc2 kinase and its
      regulatory subunit cyclin B is required for the phosphorylation of the Ki-67
      protein. We further demonstrated that the Ki-67 protein is a new member of the
      family of MPM-2 reactive phosphoproteins, which includes both structural and
      functional proteins that are necessary for the control and timing of mitosis.
      Phosphorylation and dephosphorylation of the Ki-67 protein are therefore
      controlled by key regulatory structures of the cell cycle and occur at two
      hallmark events within the cell cycle: the breakdown and the reorganization of
      the nucleus during mitosis.
CI  - Copyright 2000 Wiley-Liss, Inc.
FAU - Endl, E
AU  - Endl E
AD  - Department of Immunology and Cell Biology, Division of Molecular Immunology,
      Research Center Borstel, Borstel, Germany.
FAU - Gerdes, J
AU  - Gerdes J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Physiol
JT  - Journal of cellular physiology
JID - 0050222
RN  - 0 (Antibodies)
RN  - 0 (Antineoplastic Agents)
RN  - 0 (Cyclin B)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Epitopes)
RN  - 0 (Ki-67 Antigen)
RN  - 0 (Phosphoproteins)
RN  - 0 (Phosphorus Radioisotopes)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
RN  - H88EPA0A3N (Staurosporine)
RN  - SH1WY3R615 (Nocodazole)
RN  - VC2W18DGKR (Thymidine)
SB  - IM
MH  - Adenosine Triphosphate/pharmacology
MH  - Anaphase/physiology
MH  - Antibodies
MH  - Antineoplastic Agents/pharmacology
MH  - CDC2 Protein Kinase/metabolism
MH  - Cyclin B/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme Inhibitors/pharmacology
MH  - Epitopes/immunology/metabolism
MH  - Flow Cytometry
MH  - Fluorescent Antibody Technique
MH  - G2 Phase/drug effects/physiology/radiation effects
MH  - HeLa Cells
MH  - Humans
MH  - Ki-67 Antigen/analysis/immunology/*metabolism
MH  - Metaphase/*physiology
MH  - Nocodazole/pharmacology
MH  - Phosphoproteins/immunology/metabolism
MH  - Phosphorus Radioisotopes
MH  - Phosphorylation
MH  - Prophase/*physiology
MH  - *Protein Processing, Post-Translational
MH  - S Phase/drug effects/physiology
MH  - Staurosporine/pharmacology
MH  - Thymidine/antagonists & inhibitors
EDAT- 2000/02/01 00:00
MHDA- 2000/02/01 00:01
CRDT- 2000/02/01 00:00
PHST- 2000/02/01 00:00 [pubmed]
PHST- 2000/02/01 00:01 [medline]
PHST- 2000/02/01 00:00 [entrez]
AID - 10.1002/(SICI)1097-4652(200003)182:3<371::AID-JCP8>3.0.CO;2-J [pii]
AID - 10.1002/(SICI)1097-4652(200003)182:3<371::AID-JCP8>3.0.CO;2-J [doi]
PST - ppublish
SO  - J Cell Physiol. 2000 Mar;182(3):371-80. doi:
      10.1002/(SICI)1097-4652(200003)182:3<371::AID-JCP8>3.0.CO;2-J.