BioEssays,
Journal Year:
2023,
Volume and Issue:
46(2)
Published: Dec. 3, 2023
Abstract
Transport
of
macromolecules
from
the
nucleus
to
cytoplasm
is
essential
for
nearly
all
cellular
and
developmental
events,
when
mis‐regulated,
associated
with
diseases,
tumor
formation/growth,
cancer
progression.
Nuclear
Envelope
(NE)‐budding
a
newly
appreciated
nuclear
export
pathway
large
macromolecular
machineries,
including
those
assembled
allow
co‐regulation
functionally
related
components,
that
bypasses
canonical
through
pores.
In
this
pathway,
complexes
are
enveloped
by
inner
membrane,
transverse
perinuclear
space,
then
exit
outer
membrane
release
its
contents
into
cytoplasm.
NE‐budding
conserved
process
shares
many
features
egress
mechanisms
used
herpesviruses.
Despite
biological
importance
clinical
relevance,
little
yet
known
about
regulatory
structural
machineries
occur
in
any
system.
Here
we
summarize
what
currently
or
proposed
intriguing
process.
Chemical Communications,
Journal Year:
2025,
Volume and Issue:
unknown
Published: Jan. 1, 2025
The
nuclear
membrane
is
a
double-layered
structure
that
physically
protects
the
cell's
DNA
from
chemical
reactions
occurring
in
other
parts
of
cell.
In
this
study,
we
present
first
brand-new
small-molecule
fluorescent
probe
selectively
stains
membrane,
allowing
for
visualization
morphology
without
interfering
with
DNA's
activity.
Current Opinion in Cell Biology,
Journal Year:
2023,
Volume and Issue:
85, P. 102230 - 102230
Published: Aug. 31, 2023
The
canonical
appearance
of
the
nucleus
depends
on
constant
adaptation
and
remodeling
nuclear
envelope
in
response
to
changing
biomechanical
forces
metabolic
demands.
Dynamic
events
at
play
a
vital
role
supporting
key
functions
as
well
conferring
plasticity
this
organelle.
Moreover,
imbalance
these
dynamic
processes
is
emerging
central
feature
disease
etiology.
This
review
focuses
recent
advances
that
shed
light
myriad
contribute
resilience
flexibility
architecture.
bioRxiv (Cold Spring Harbor Laboratory),
Journal Year:
2023,
Volume and Issue:
unknown
Published: April 27, 2023
Nuclear
pore
complexes
(NPCs)
regulate
information
transfer
between
the
nucleus
and
cytoplasm.
NPC
defects
are
linked
to
several
neurological
diseases,
but
processes
governing
biogenesis
spatial
organization
poorly
understood.
Here,
we
identify
a
temporal
window
of
strongly
upregulated
during
neuronal
maturation.
We
demonstrate
that
AAA+
protein
torsinA,
whose
loss
function
causes
neurodevelopmental
movement
disorder
DYT-TOR1A
(DYT1)
dystonia,
coordinates
this
period
without
impacting
total
density.
Using
new
mouse
line
in
which
endogenous
Nup107
is
Halo-Tagged,
find
torsinA
essential
for
correct
localization
formation.
In
absence
inner
nuclear
membrane
buds
excessively
at
sites
mislocalized,
nascent
NPCs,
assembly
completion
delayed.
Our
work
implies
number
independently
regulated
suggests
critical
normal
kinetics
NPCs.
bioRxiv (Cold Spring Harbor Laboratory),
Journal Year:
2024,
Volume and Issue:
unknown
Published: Sept. 23, 2024
ABSTRACT/SUMMARY
Herpesvirales
are
an
ancient
viral
order
that
infects
species
from
mollusks
to
humans
for
life.
During
infection,
these
viruses
translocate
their
large
capsids
the
nucleus
cytoplasm
independently
canonical
route
through
nuclear
pore.
Instead,
dock
at
inner
membrane
and
bud
into
perinuclear
space.
These
enveloped
virions
fuse
with
outer
releasing
maturation
infectious
virions.
The
budding
stage
is
mediated
by
virally
encoded
proteins.
But
mediator
of
subsequent
fusion
unknown.
Here,
using
a
whole-genome
CRISPR
screen
herpes
simplex
virus
1,
we
identified
CLCC1
as
essential
host
factor
egress.
Loss
results
in
defect
egress,
accumulation
capsid-containing
vesicles,
drop
titers.
In
uninfected
cells,
loss
causes
pore
complex
insertion.
Viral
homologs
present
herpesviruses
infect
fish.
Our
findings
uncover
cellular
mechanism
important
fundamental
process
envelope
morphogenesis
hijack
capsid
transport.
