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Vol. 13, Issue 10, 3627-3645, October 2002
*Molecular Medicine Unit, University of Leeds, Clinical Sciences
Building, St. James's University Hospital, Leeds LS9 7TF, United
Kingdom; and Departments of EB1 is a microtubule tip-associated protein that interacts with
the APC tumor suppressor protein and components of the dynein/dynactin complex. We have found that the C-terminal 50 and 84 amino acids (aa) of EB1 were sufficient to mediate the interactions
with APC and dynactin, respectively. EB1 formed mutually exclusive
complexes with APC and dynactin, and a direct interaction between EB1
and p150Glued was identified. EB1-GFP deletion
mutants demonstrated a role for the N-terminus in mediating the
EB1-microtubule interaction, whereas C-terminal regions contributed to
both its microtubule tip localization and a centrosomal localization.
Cells expressing the last 84 aa of EB1 fused to GFP (EB1-C84-GFP)
displayed profound defects in microtubule organization and centrosomal
anchoring. EB1-C84-GFP expression severely inhibited microtubule
regrowth, focusing, and anchoring in transfected cells during recovery
from nocodazole treatment. The recruitment of Biological Sciences and
§Chemistry and Biochemistry, University of Notre Dame,
Notre Dame, Indiana 46556
-tubulin and
p150Glued to centrosomes was also inhibited.
None of these effects were seen in cells expressing the last 50 aa of
EB1 fused to GFP. Furthermore, EB1-C84-GFP expression did not induce
Golgi apparatus fragmentation. We propose that a functional interaction
between EB1 and p150Glued is required for
microtubule minus end anchoring at centrosomes during the assembly and
maintenance of a radial microtubule array.
Corresponding author. E-mail address:
rmrjma{at}leeds.ac.uk.
¶
Present address: CRUK Clinical Center at Leeds,
Division of Cancer Medicine Research, St. James's University Hospital,
Leeds LS9 7TF, United Kingdom.
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