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Vol. 12, Issue 7, 1995-2009, July 2001
*Department of Biology, University of North Carolina, Chapel Hill,
North Carolina 27599-3280; and The ability of kinetochores to recruit microtubules,
generate force, and activate the mitotic spindle checkpoint may all
depend on microtubule- and/or tension-dependent changes in
kinetochore assembly. With the use of quantitative digital
imaging and immunofluorescence microscopy of PtK1 tissue cells, we find
that the outer domain of the kinetochore, but not the
CREST-stained inner core, exhibits three microtubule-dependent
assembly states, not directly dependent on tension. First, prometaphase
kinetochores with few or no kinetochore microtubules have abundant punctate or oblate fluorescence morphology when stained for outer domain motor proteins CENP-E and
cytoplasmic dynein and checkpoint proteins BubR1 and Mad2. Second,
microtubule depolymerization induces expansion of the
kinetochore outer domain into crescent and ring
morphologies around the centromere. This expansion may enhance
recruitment of kinetochore microtubules, and occurs with
more than a 20- to 100-fold increase in dynein and relatively little
change in CENP-E, BubR1, and Mad2 in comparison to prometaphase
kinetochores. Crescents disappear and dynein decreases substantially upon microtubule reassembly. Third, when
kinetochores acquire their full metaphase complement of
kinetochore microtubules, levels of CENP-E, dynein, and
BubR1 decrease by three- to sixfold in comparison to unattached
prometaphase kinetochores, but remain detectable. In
contrast, Mad2 decreases by 100-fold and becomes undetectable,
consistent with Mad2 being a key factor for the "wait-anaphase"
signal produced by unattached kinetochores. Like previously
found for Mad2, the average amounts of CENP-E, dynein, or BubR1 at
metaphase kinetochores did not change with the loss of
tension induced by taxol stabilization of microtubules.
Fox Chase Cancer Center,
Philadelphia, Pennsylvania
Corresponding author. E-mail address:
tsalmon{at}emailunc.edu.
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