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Vol. 14, Issue 1, 107-117, January 2003
throughout the Mammalian Cell Cycle
Wellcome Trust Biocentre, University of Dundee, Dundee DD1
5EH, United Kingdom
Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine
phosphatase that regulates many cellular processes, including cell
division. When transiently expressed as fluorescent protein (FP)
fusions, the three PP1 isoforms, 
, 
/
, and 
1, are active phosphatases with distinct localization patterns. We report here the
establishment and characterization of HeLa cell lines stably expressing
either FP-PP1 or FP alone. Time-lapse imaging reveals dynamic
targeting of FP-PP1 to specific sites throughout the cell cycle,
contrasting with the diffuse pattern observed for FP alone. FP-PP1
shows a nucleolar accumulation during interphase. On entry into
mitosis, it localizes initially at kinetochores, where it
exchanges rapidly with the diffuse cytoplasmic pool. A dramatic
relocalization of PP1 to the chromosome-containing regions occurs at
the transition from early to late anaphase, and by telophase FP-PP1
also accumulates at the cleavage furrow and midbody. The changing
spatio-temporal distribution of PP1 revealed using the stable PP1
cell lines implicates it in multiple processes, including nucleolar
function, the regulation of chromosome segregation and cytokinesis.
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