PMID- 10574707
OWN - NLM
STAT- MEDLINE
DCOM- 20000424
LR  - 20161124
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 112 ( Pt 24)
DP  - 1999 Dec
TI  - Cell cycle regulation of PML modification and ND10 composition.
PG  - 4581-8
AB  - The nuclear sub-structures known as ND10, PODs or PML nuclear bodies can be
      rapidly modified by diverse stimuli, and the resultant structural changes
      correlate with events such as cellular transformation and successful virus
      infection. We show that the ND10 components PML and Sp100 undergo profound
      biochemical changes during the cell cycle. Both proteins are conjugated to the
      ubiquitin-like protein SUMO-1 during interphase, but they become de-conjugated
      during mitosis and an isoform of PML of distinct electrophoretic mobility
      appears. This mitosis-specific form of PML is highly labile in vitro, but is
      partially stabilised by phosphatase inhibitors. Treatment of interphase cells
      with phosphatase inhibitors induces the production of a PML isoform of similar
      gel mobility to the mitosis-specific species, and taken together these results
      suggest that phosphorylation is an important factor in the differential
      modification of PML during the cell cycle. PML and Sp100 normally tightly
      co-localise in ND10 in interphase cells, but they become separated during
      mitosis. Interphase cells treated with phosphatase inhibitors or subjected to
      heat shock also show structural changes in ND10, accompanied by alterations to
      the normal pattern of PML modification. Taken with previous findings on the
      effects of infection by herpes simplex virus and adenovirus on ND10 structure and
      PML modification, these results suggest that the many factors which have been
      shown to modify ND10 structure may do so by interaction with the biochemical
      mechanisms that act on ND10 components during the cell cycle.
FAU - Everett, R D
AU  - Everett RD
AD  - MRC Virology Unit, Church Street, Glasgow G11 5JR, Scotland, UK.
      r.everett@vir.gla.ac.uk
FAU - Lomonte, P
AU  - Lomonte P
FAU - Sternsdorf, T
AU  - Sternsdorf T
FAU - van Driel, R
AU  - van Driel R
FAU - Orr, A
AU  - Orr A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Protein Isoforms)
RN  - 0 (SUMO-1 Protein)
RN  - 0 (Ubiquitins)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - Cell Cycle/*physiology
MH  - Cell Division
MH  - Cell Line
MH  - Cell Nucleus/drug effects/metabolism/*ultrastructure
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme Inhibitors/pharmacology
MH  - Heat-Shock Response
MH  - Humans
MH  - Phosphoric Monoester Hydrolases/antagonists & inhibitors
MH  - Protein Isoforms/metabolism
MH  - SUMO-1 Protein
MH  - Ubiquitins/metabolism
EDAT- 1999/11/27 09:00
MHDA- 2000/04/29 09:00
CRDT- 1999/11/27 09:00
PHST- 1999/11/27 09:00 [pubmed]
PHST- 2000/04/29 09:00 [medline]
PHST- 1999/11/27 09:00 [entrez]
PST - ppublish
SO  - J Cell Sci. 1999 Dec;112 ( Pt 24):4581-8.