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Vol. 13, Issue 10, 3614-3626, October 2002
and
*Department of Cell Biology, Harvard Medical School, Boston,
Massachusetts 02115; and EB1 targets to polymerizing microtubule ends, where it is favorably
positioned to regulate microtubule polymerization and confer molecular
recognition of the microtubule end. In this study, we focus on two
aspects of the EB1-microtubule interaction: regulation of microtubule
dynamics by EB1 and the mechanism of EB1 association with microtubules.
Immunodepletion of EB1 from cytostatic factor-arrested M-phase
Xenopus egg extracts dramatically reduced microtubule length; this was complemented by readdition of EB1. By time-lapse microscopy, EB1 increased the frequency of microtubule rescues and
decreased catastrophes, resulting in increased polymerization and
decreased depolymerization and pausing. Imaging of EB1 fluorescence revealed a novel structure: filamentous extensions on microtubule plus
ends that appeared during microtubule pauses; loss of these extensions
correlated with the abrupt onset of polymerization. Fluorescent EB1
localized to comets at the polymerizing plus ends of microtubules in
cytostatic factor extracts and uniformly along the lengths of
microtubules in interphase extracts. The temporal decay of EB1
fluorescence from polymerizing microtubule plus ends predicted a
dissociation half-life of seconds. Fluorescence recovery after
photobleaching also revealed dissociation and rebinding of EB1 to the
microtubule wall with a similar half-life. EB1 targeting to
microtubules is thus described by a combination of higher affinity binding to polymerizing ends and lower affinity binding along the wall,
with continuous dissociation. The latter is likely to be attenuated in
interphase. The highly conserved effect of EB1 on microtubule dynamics
suggests it belongs to a core set of regulatory factors conserved in
higher organisms, and the complex pattern of EB1 targeting to
microtubules could be exploited by the cell for coordinating
microtubule behaviors.
Department of Biology,
University of North Carolina at Chapel Hill, Chapel Hill, North
Carolina 27599
Corresponding author. E-mail address:
jennifer_tirnauer{at}hms.harvard.edu.
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