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Novel septin 9 repeat motifs altered in neuralgic amyotrophy bind and bundle microtubules.
[neuralgic amyotrophy]
Septin
9
(
SEPT
9
)
interacts
with
microtubules
(
MTs
)
and
is
mutated
in
hereditary
neuralgic
amyotrophy
(
HNA
)
,
an
autosomal-dominant
neuropathy
.
The
mechanism
of
SEPT
9
interaction
with
MTs
and
the
molecular
basis
of
HNA
are
unknown
.
Here
,
we
show
that
the
N-
terminal
domain
of
SEPT
9
contains
the
novel
repeat
motifs
K
/
R-
x-x-
E
/
D
and
R
/
K-R-x-
E
,
which
bind
and
bundle
MTs
by
interacting
with
the
acidic
C-
terminal
tails
of
β-tubulin
.
Alanine
scanning
mutagenesis
revealed
that
the
K
/
R-R
/
x-x-
E
/
D
motifs
pair
electrostatically
with
one
another
and
the
tails
of
β-tubulin
,
enabling
septin–septin
interactions
that
link
MTs
together
.
SEPT
9
isoforms
lacking
repeat
motifs
or
containing
the
HNA-linked
mutation
R
88
W
,
which
maps
to
the
R
/
K-R-x-
E
motif
,
diminished
intracellular
MT
bundling
and
impaired
asymmetric
neurite
growth
in
PC
-
12
cells
.
Thus
,
the
SEPT
9
repeat
motifs
bind
and
bundle
MTs
,
and
thereby
promote
asymmetric
neurite
growth
.
These
results
provide
the
first
insight
into
the
mechanism
of
septin
interaction
with
MTs
and
the
molecular
and
cellular
basis
of
HNA
.
Diseases
Validation
Diseases presenting
"asymmetric neurite growth"
symptom
neuralgic amyotrophy
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