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Vol. 14, Issue 4, 1405-1417, April 2003
Department of Physiology, University of Pennsylvania
School of Medicine, Philadelphia, Pennsylvania 19104-6085
Several microtubule-binding proteins including EB1, dynactin, APC,
and CLIP-170 localize to the plus-ends of growing microtubules. Although these proteins can bind to microtubules independently, evidence for interactions among them has led to the hypothesis of a
plus-end complex. Here we clarify the interaction between EB1 and
dynactin and show that EB1 binds directly to the N-terminus of the
p150Glued subunit. One function of a plus-end complex may
be to regulate microtubule dynamics. Overexpression of either EB1 or
p150Glued in cultured cells bundles microtubules,
suggesting that each may enhance microtubule stability. The morphology
of these bundles, however, differs dramatically, indicating that EB1
and dynactin may act in different ways. Disruption of the dynactin
complex augments the bundling effect of EB1, suggesting that dynactin may regulate the effect of EB1 on microtubules. In vitro assays were
performed to elucidate the effects of EB1 and p150Glued on
microtubule polymerization, and they show that p150Glued
has a potent microtubule nucleation effect, whereas EB1 has a potent
elongation effect. Overall microtubule dynamics may result from a
balance between the individual effects of plus-end proteins. Differences in the expression and regulation of plus-end proteins in
different cell types may underlie previously noted differences in
microtubule dynamics.
Corresponding author. E-mail address:
holzbaur{at}mail.med.upenn.edu.
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