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Vol. 10, Issue 4, 1105-1118, April 1999
and§
Departments of *Pathology and Posttranslationally modified forms of tubulin accumulate in the
subset of stabilized microtubules (MTs) in cells but are not themselves involved in generating MT stability. We showed previously that stabilized, detyrosinated (Glu) MTs function to localize vimentin intermediate filaments (IFs) in fibroblasts. To
determine whether tubulin detyrosination or MT stability is the
critical element in the preferential association of IFs with Glu MTs,
we microinjected nonpolymerizable Glu tubulin into cells. If
detyrosination is critical, then soluble Glu tubulin should be a
competitive inhibitor of the IF-MT interaction. Before microinjection,
Glu tubulin was rendered nonpolymerizable and nontyrosinatable by treatment with iodoacetamide (IAA). Microinjected IAA-Glu tubulin disrupted the interaction of IFs with MTs, as assayed by the collapse of IFs to a perinuclear location, and had no detectable effect on the
array of Glu or tyrosinated MTs in cells. Conversely, neither IAA-tyrosinated tubulin nor untreated Glu tubulin, which assembled into
MTs, caused collapse of IFs when microinjected. The epitope on Glu
tubulin responsible for interfering with the Glu MT-IF interaction was
mapped by microinjecting tubulin fragments of Anatomy and Cell
Biology, Columbia University, College of Physicians and Surgeons, New
York, New York 10032
-tubulin. The 14-kDa
C-terminal fragment of Glu tubulin (-C Glu) induced IF collapse,
whereas the 36-kDa N-terminal fragment of -tubulin did not alter the
IF array. The epitope required more than the detyrosination site at the
C terminus, because a short peptide (a 7-mer) mimicking the C terminus
of Glu tubulin did not disrupt the IF distribution. We previously
showed that kinesin may mediate the interaction of Glu MTs and IFs. In
this study we found that kinesin binding to MTs in vitro was inhibited by the same reagents (i.e., IAA-Glu tubulin and -C Glu) that disrupted the IF-Glu MT interaction in vivo. These results demonstrate for the first time that tubulin detyrosination functions as a signal
for the recruitment of IFs to MTs via a mechanism that is likely to
involve kinesin.
Present address: Department of
Ophthalmology, Dyson Institute for Vision Research, Cornell University
Medical College, New York, NY 10021.
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