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One size does not fit all: the oligomeric states of αB crystallin.
[alexander disease]
Small
Heat
Shock
Proteins
(
sHSPs
)
are
a
diverse
family
of
molecular
chaperones
that
delay
protein
aggregation
through
interactions
with
non-native
and
aggregate-prone
protein
states
.
This
function
has
been
shown
to
be
important
to
cellular
viability
and
sHSP
function
/
dysfunction
is
implicated
in
many
diseases
,
including
Alzheimer
's
and
Alexander
disease
.
Though
their
gene
products
are
small
,
many
sHSPs
assemble
into
a
distribution
of
large
oligomeric
states
that
undergo
dynamic
subunit
exchange
.
These
inherent
properties
present
significant
experimental
challenges
for
characterizing
sHSP
oligomers
.
Of
the
human
sHSPs
,
αB
crystallin
is
a
paradigm
example
of
sHSP
oligomeric
properties
.
Advances
in
our
understanding
of
sHSP
structure
,
oligomeric
distribution
,
and
dynamics
have
prompted
the
proposal
of
several
models
for
the
oligomeric
states
of
αB
.
The
aim
of
this
review
is
to
highlight
characteristics
of
αB
crystallin
(
αB
)
that
are
key
to
understanding
its
structure
and
function
.
The
current
state
of
knowledge
,
existing
models
,
and
outstanding
questions
that
remain
to
be
addressed
are
presented
.
