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Volume 272, Number 51, Issue of December 19, 1997
pp. 32011-32018
(Received for publication, August 13, 1997, and in revised form, October 6, 1997)
From the Department of Chemistry and Biochemistry and the Center
for Molecular Genetics, University of California, San Diego,
La Jolla, California 92093-0367
The evolutionarily conserved multisubunit complex
known as the cyclosome or anaphase-promoting complex is involved in
catalyzing the ubiquitination of diverse substrates in M phase,
allowing their destruction by the 26 S proteasome and the completion
of mitosis. Three of the eight subunits of the anaphase-promoting complex (CDC16, CDC23, and CDC27) have been shown to be phosphorylated in M phase, and their phosphorylation is required for the
anaphase-promoting complex to be active as a ubiquitin ligase. Several
subunits of the anaphase-promoting complex contain tetratricopeptide
repeats, a protein motif involved in protein/protein interactions. PP5 is a serine/threonine phosphatase that also contains four copies of the
tetratricopeptide repeats motif. Here we show by a combination of
two-hybrid analysis and in vitro binding that PP5 interacts with CDC16 and CDC27, two subunits of the anaphase-promoting complex. Only the NH2-terminal domain of PP5, containing all four
tetratricopeptide repeats, is required for this physical interaction.
Deletion analysis suggests that the site of binding to PP5 is localized
to the COOH-terminal block of tetratricopeptide repeats in CDC16 and
CDC27. In addition, indirect immunofluorescence showed that PP5
localizes to the mitotic spindle apparatus. The direct interaction of
PP5 with CDC16 and CDC27, as well as its overlapping spindle
localization in mitosis, suggests that PP5 may be involved in the
regulation of the activity of the anaphase-promoting complex.
The Serine/Threonine Phosphatase PP5 Interacts with CDC16 and
CDC27, Two Tetratricopeptide Repeat-containing Subunits of the
Anaphase-promoting Complex
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