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Vol. 12, Issue 9, 2870-2880, September 2001
and
*Department of Molecular Biology and Genetics, Cornell University,
Ithaca, New York 14853-2703; Stu2p is a member of a conserved family of microtubule-binding
proteins and an essential protein in yeast. Here, we report the first
in vivo analysis of microtubule dynamics in cells lacking a member of
this protein family. For these studies, we have used a conditional
Stu2p depletion strain expressing Department of Biology,
University of North Carolina-Chapel Hill, Chapel Hill, North Carolina
27599-3280; and §MRC Laboratory of Molecular Biology,
Cambridge CB2 2QH, United Kingdom
-tubulin fused to green
fluorescent protein. Depletion of Stu2p leads to fewer and less dynamic
cytoplasmic microtubules in both G1 and preanaphase cells. The
reduction in cytoplasmic microtubule dynamics is due primarily to
decreases in both the catastrophe and rescue frequencies and an
increase in the fraction of time microtubules spend pausing. These
changes have significant consequences for the cell because they impede
the ability of cytoplasmic microtubules to orient the spindle. In
addition, recovery of fluorescence after photobleaching indicates that
kinetochore microtubules are no longer dynamic in the
absence of Stu2p. This deficiency is correlated with a failure to
properly align chromosomes at metaphase. Overall, we provide evidence
that Stu2p promotes the dynamics of microtubule plus-ends in vivo and
that these dynamics are critical for microtubule interactions with
kinetochores and cortical sites in the cytoplasm.
Whitehead Institute for
Biomedical Research, Cambridge, MA 02142-1479;
Wellcome/CRC Institute of Cancer and Developmental
Biology, Cambridge University, Cambridge CB2 1QR, United Kingdom.
¶
Corresponding author. E-mail address:
tch4{at}cornell.edu.
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