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Vol. 12, Issue 10, 3103-3113, October 2001
§ and
Actin polymerization is accompanied by the formation of protein
complexes that link extracellular signals to sites of actin assembly
such as membrane ruffles and focal adhesions. One candidate recently
implicated in these processes is the LIM domain protein zyxin, which
can bind both Ena/vasodilator-stimulated phosphoprotein (VASP) proteins
and the actin filament cross-linking protein Department of Cell Biology, Gesellschaft
für Biotechnologische Forschung, D-38124 Braunschweig, Germany;
and Department of Cell Biology, Austrian Academy of
Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria
-actinin. To
characterize the localization and dynamics of zyxin in detail, we
generated both monoclonal antibodies and a green fluorescent protein
(GFP)-fusion construct. The antibodies colocalized with ectopically
expressed GFP-VASP at focal adhesions and along stress fibers, but
failed to label lamellipodial and filopodial tips, which also recruit
Ena/VASP proteins. Likewise, neither microinjected, fluorescently
labeled zyxin antibodies nor ectopically expressed GFP-zyxin were
recruited to these latter sites in live cells, whereas both probes
incorporated into focal adhesions and stress fibers. Comparing the
dynamics of zyxin with that of the focal adhesion protein vinculin
revealed that both proteins incorporated simultaneously into newly
formed adhesions. However, during spontaneous or induced focal adhesion
disassembly, zyxin delocalization preceded that of either vinculin or
paxillin. Together, these data identify zyxin as an early target for
signals leading to adhesion disassembly, but exclude its role in
recruiting Ena/VASP proteins to the tips of lamellipodia and filopodia.
Online version of this article contains
video material for Figure 3, 4, 5, and 7. Online version is available
at www.molbiolcell.org.
*
K.R. and M.K. contributed equally to this work.
§
Present address: Department of Biology,
Massachusetts Institute of Technology, Cambridge, MA 02138-4307.
Corresponding author. E-mail address:
jwe{at}gbf.de.
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