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Steve Rogers and Ron Vale
Over the last few years, it has become evident that there is
a growing class of microtubule-associated proteins (MAPs) that localize to growing
MT plus ends in vivo. This localization is significant as it allows these
proteins to modulate microtubule dynamics, mediate interactions between the
microtubule tip and other cellular structures, and localize other 'passenger'
proteins to the microtubule plus end. The EB1 family of proteins are one such
class of plus end-binding MAP. First identified as a binding partner for the
human adenomatous polyposis coli (APC) tumor suppressor protein, the EB1s have
since been shown to be evolutionarily conserved from yeast to mammals. We have
been studying the cellular functions of EB1 using cultured Drosophila Schneider
(S2) cells as a model system. We find that, as in other systems, fly EB1 localizes
to the tips of microtubules and to the centrosomes and spindle poles throughout
the cell cycle. The use of RNAi to generate EB1 loss-of-function phenotypes
revealed that interphase microtubule organization appeared normal. However,
EB1-deficient mitotic cells exhibit an array of spindle defects, along with
an elevated mitotic index. In addition, mitotic spindles, which usually self-
center within these cells, often misposition away from the cell center. We also
examined the contribution of EB1 to microtubule dynamics in vivo using newly-developed
methods in fly cells.
ASCB 2001
last updated 1/7/02
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