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The F-BAR protein PSTPIP1 controls extracellular matrix degradation and filopodia formation in macrophages.
[wiskott-aldrich syndrome]
PSTPIP
1
is
a
cytoskeletal
adaptor
and
F-BAR
protein
that
has
been
implicated
in
autoinflammatory
disease
,
most
notably
in
the
PAPA
syndrome
:
pyogenic
sterile
arthritis
,
pyoderma
gangrenosum
,
and
acne
.
However
,
the
mechanism
by
which
PSTPIP
1
regulates
the
actin
cytoskeleton
and
contributes
to
disease
pathogenesis
remains
elusive
.
Here
,
we
show
that
endogenous
PSTPIP
1
negatively
regulates
macrophage
podosome
organization
and
matrix
degradation
.
We
identify
a
novel
PSTPIP
1
-
R
405
C
mutation
in
a
patient
presenting
with
aggressive
pyoderma
gangrenosum
.
Identification
of
this
mutation
reveals
that
PSTPIP
1
regulates
the
balance
of
podosomes
and
filopodia
in
macrophages
.
The
PSTPIP
1
-
R
405
C
mutation
is
in
the
SRC
homology
3
(
SH
3
)
domain
and
impairs
Wiskott-
Aldrich
syndrome
protein
(
WASP
)
binding
,
but
it
does
not
affect
interaction
with
protein-tyrosine
phosphatase
(
PTP
)
-
PEST
.
Accordingly
,
WASP
inhibition
reverses
the
elevated
F-
actin
content
,
filopodia
formation
,
and
matrix
degradation
induced
by
PSTPIP
1
-
R
405
C
.
Our
results
uncover
a
novel
role
for
PSTPIP
1
and
WASP
in
orchestrating
different
types
of
actin-based
protrusions
.
Our
findings
implicate
the
cytoskeletal
regulatory
functions
of
PSTPIP
1
in
the
pathogenesis
of
pyoderma
gangrenosum
and
suggest
that
the
cytoskeleton
is
a
rational
target
for
therapeutic
intervention
in
autoinflammatory
disease
.
Diseases
Validation
Diseases presenting
"pyoderma gangrenosum"
symptom
malignant atrophic papulosis
wiskott-aldrich syndrome
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