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Vol. 13, Issue 7, 2301-2310, July 2002
Adolf-Butenandt-Institut/Zellbiologie,
Ludwig-Maximilians-Universität München, D-80336 Munich,
Germany
EB1 proteins are ubiquitous microtubule-associated proteins
involved in microtubule search and capture, regulation of microtubule dynamics, cell polarity, and chromosome stability. We have cloned a
complete cDNA of Dictyostelium EB1 (DdEB1), the largest
known EB1 homolog (57 kDa). Immunofluorescence analysis and expression of a green fluorescent protein-DdEB1 fusion protein revealed
that DdEB1 localizes along microtubules, at microtubule tips,
centrosomes, and protruding pseudopods. During mitosis, it was found at
the spindle, spindle poles, and kinetochores. DdEB1 is the
first EB1-homolog that is also a genuine centrosomal component, because
it was localized at isolated centrosomes that are free of microtubules.
Furthermore, centrosomal DdEB1 distribution was unaffected by
nocodazole treatment. DdEB1 colocalized with DdCP224, the XMAP215
homolog, at microtubule tips, the centrosome, and
kinetochores. Furthermore, both proteins were part of the
same cytosolic protein complex, suggesting that they may act together
in their functions. DdEB1 deletion mutants expressed as green
fluorescent protein or maltose-binding fusion proteins indicated that
microtubule binding requires homo-oligomerization, which is mediated by
a coiled-coil domain. A DdEB1 null mutant was viable but retarded in
prometaphase progression due to a defect in spindle formation. Because
spindle elongation was normal, DdEB1 seems to be required for the
initiation of the outgrowth of spindle microtubules.
Online version of this
article contains video material for some figures. Online version
available at www.molbiolcell.org.
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