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Processive acceleration of actin barbed-end assembly by N-WASP.
[wiskott-aldrich syndrome]
Neuronal
Wiskott-
Aldrich
syndrome
protein
(
N-WASP
)
-
activated
actin
polymerization
drives
extension
of
invadopodia
and
podosomes
into
the
basement
layer
.
In
addition
to
activating
Arp
2
/
3
,
N-WASP
binds
actin-filament
barbed
ends
,
and
both
N-WASP
and
barbed
ends
are
tightly
clustered
in
these
invasive
structures
.
We
use
nanofibers
coated
with
N-WASP
WWCA
domains
as
model
cell
surfaces
and
single
-actin-filament
imaging
to
determine
how
clustered
N-WASP
affects
Arp
2
/
3
-
independent
barbed-end
assembly
.
Individual
barbed
ends
captured
by
WWCA
domains
grow
at
or
below
their
diffusion-
limited
assembly
rate
.
At
high
filament
densities
,
however
,
overlapping
filaments
form
buckles
between
their
nanofiber
tethers
and
myosin
attachment
points
.
These
buckles
grew
∼
3
.
4
-
fold
faster
than
the
diffusion-
limited
rate
of
unattached
barbed
ends
.
N-WASP
constructs
with
and
without
the
native
polyproline
(
PP
)
region
show
similar
rate
enhancements
in
the
absence
of
profilin
,
but
profilin
slows
barbed-end
acceleration
from
constructs
containing
the
PP
region
.
Increasing
Mg
(
2
+
)
to
enhance
filament
bundling
increases
the
frequency
of
filament
buckle
formation
,
consistent
with
a
requirement
of
accelerated
assembly
on
barbed-end
bundling
.
We
propose
that
this
novel
N-WASP
assembly
activity
provides
an
Arp
2
/
3
-
independent
force
that
drives
nascent
filament
bundles
into
the
basement
layer
during
cell
invasion
.
Diseases
Validation
Diseases presenting
"single-actin-filament imaging"
symptom
wiskott-aldrich syndrome
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