Mechanisms, regulation and functions of the unfolded protein response
Nature Reviews Molecular Cell Biology,
Год журнала:
2020,
Номер
21(8), С. 421 - 438
Опубликована: Май 26, 2020
Язык: Английский
Hallmarks of Health
Cell,
Год журнала:
2020,
Номер
184(1), С. 33 - 63
Опубликована: Дек. 18, 2020
Язык: Английский
Autophagy and the hallmarks of aging
Ageing Research Reviews,
Год журнала:
2021,
Номер
72, С. 101468 - 101468
Опубликована: Сен. 24, 2021
Язык: Английский
Functional Modules of the Proteostasis Network
Cold Spring Harbor Perspectives in Biology,
Год журнала:
2019,
Номер
12(1), С. a033951 - a033951
Опубликована: Март 4, 2019
Gopal
G.
Jayaraj,
Mark
S.
Hipp
and
F.
Ulrich
Hartl
Department
of
Cellular
Biochemistry,
Max
Planck
Institute
Am
Klopferspitz
18,
82152
Martinsried,
Germany
Correspondence:
uhartl{at}biochem.mpg.de
Язык: Английский
Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges
Journal of Biological Chemistry,
Год журнала:
2022,
Номер
298(5), С. 101796 - 101796
Опубликована: Март 3, 2022
All
cells
possess
an
internal
stress
response
to
cope
with
environmental
and
pathophysiological
challenges.
Upon
stress,
reprogram
their
molecular
functions
activate
a
survival
mechanism
known
as
the
heat
shock
response,
which
mediates
rapid
induction
of
chaperones
such
proteins
(HSPs).
This
potent
production
overcomes
general
suppression
gene
expression
results
in
high
levels
HSPs
subsequently
refold
or
degrade
misfolded
proteins.
Once
damage
is
repaired
removed,
terminate
resume
regular
functions.
Thus,
fulfillment
requires
swift
robust
coordination
between
activation
completion
that
determined
by
status
cell.
In
recent
years,
single-cell
fluorescence
microscopy
techniques
have
begun
be
used
unravelling
HSP-gene
pathways,
from
DNA
transcription
mRNA
degradation.
this
review,
we
will
address
mechanisms
different
organisms
cell
types
coordinate
signaling
networks
act
transcription,
translation,
decay
ensure
protein
quality
control.
For
grow
function
properly,
they
must
maintain
specific
cellular
conditions
allow
acquire
functional
conformations
achieve
homeostasis
(proteostasis)
(1Gasch
A.P.
Spellman
P.T.
Kao
C.M.
Carmel-Harel
O.
Eisen
M.B.
Storz
G.
Botstein
D.
Brown
P.O.
Genomic
programs
yeast
changes.Mol.
Biol.
Cell.
2000;
11:
4241-4257Crossref
PubMed
Google
Scholar).
Maintaining
proteostasis
becomes
critical
when
facing
abrupt
changes
external
conditions,
increase
temperature,
can
lead
misfolding
aggregation,
consequently,
dysfunction
(2van
Oosten-Hawle
P.
Morimoto
R.I.
Organismal
proteostasis:
Role
cell-nonautonomous
regulation
transcellular
chaperone
signaling.Genes
Dev.
2014;
28:
1533-1543Crossref
Scopus
(60)
sense,
rapidly
respond,
adapt
new
for
survival.
Organisms
bacteria
mammals
evolved
similar
varying
responses
successfully.
Some
these
strategies
include
modulations
cascades,
transcriptional
programs,
posttranslational
modifications,
dynamic
assembly
RNA
condensates
(ribonucleoprotein
[RNP]
granules)
through
liquid–liquid
phase
separation
Scholar,
3de
la
Fuente
M.
Valera
S.
Martínez-Guitarte
J.L.
ncRNAs
thermoregulation:
A
view
prokaryotes
eukaryotes.FEBS
Lett.
2012;
586:
4061-4069Crossref
(0)
4Protter
D.S.W.
Parker
R.
Principles
properties
granules.Trends
Cell
2016;
26:
668-679Abstract
Full
Text
PDF
(621)
5Pohl
C.
Dikic
I.
Cellular
control
ubiquitin-proteasome
system
autophagy.Science.
2019;
366:
818-822Crossref
(267)
6Pomatto
L.C.D.
Davies
K.J.A.
The
role
declining
adaptive
ageing.J.
Physiol.
2017;
595:
7275-7309Crossref
(76)
7Yasuda
Tsuchiya
H.
Kaiho
A.
Guo
Q.
Ikeuchi
K.
Endo
Arai
N.
Ohtake
F.
Murata
Inada
T.
Baumeister
W.
Fernández-Busnadiego
Tanaka
Saeki
Y.
Stress-
ubiquitylation-dependent
proteasome.Nature.
2020;
578:
296-300Crossref
(84)
Several
converge
sustain
sudden
acute
conditions.
Increases
temperature
universal
challenge
encountered
most
organisms.
historical
reasons,
thermal
has
been
paradigm
study
response.
Nowadays,
studies
additional
relevance
due
increased
exposure
heatwaves
derived
climate
change
(8Tomanek
L.
importance
physiological
limits
determining
biogeographical
range
shifts
global
change:
heat-shock
response.Physiol.
Biochem.
Zool.
2008;
81:
709-717Crossref
(114)
9Kassahn
K.S.
Crozier
R.H.
Pörtner
H.O.
Caley
M.J.
Animal
performance
stress:
Responses
tolerance
at
biological
organisation.Biol.
Rev.
Camb.
Philos.
Soc.
2009;
84:
277-292Crossref
(174)
10Sengupta
Garrity
Sensing
temperature.Curr.
2013;
23:
R304-R307Abstract
(72)
Increased
energy
result
heat-induced
denaturation
thermally
altered
metabolic
activity
leading
reactive
oxygen
species,
all
macromolecules,
including
(11Somero
G.N.
temperature:
Function,
regulation,
evolution.J.
Exp.
Zool
Ecol.
Integr.
333:
379-397Crossref
(44)
Cells
load
unfolded
modulating
chaperones,
also
(HSPs)
(12Parsell
D.A.
Lindquist
tolerance:
Degradation
reactivation
damaged
proteins.Annu.
Genet.
1993;
27:
437-496Crossref
13Kültz
Molecular
evolutionary
basis
OF
response.Annu.
2005;
67:
225-257Crossref
(977)
14Daugaard
Rohde
Jäättelä
70
family:
Highly
homologous
overlapping
distinct
functions.FEBS
2007;
581:
3702-3710Crossref
(830)
15Rosenzweig
Nillegoda
N.B.
Mayer
M.P.
Bukau
B.
Hsp70
network.Nat.
Mol.
20:
665-680Crossref
(295)
(HSR)
refers
HSPs,
it
common
widely
studied
stress.
play
central
lifecycle
because
promote
folding
nascent
polypeptides
into
native/functional
configurations
prevent
aggregation
16Morimoto
response:
Systems
biology
proteotoxic
aging
disease.Cold
Spring
Harb.
Symp.
Quant
2011;
76:
91-99Crossref
(263)
collaborate
mechanisms,
system,
autophagy,
target
aggregates
whose
native
state
cannot
recovered
degradation
(5Pohl
17Wang
Le
W.D.
Autophagy
system.Adv.
Med.
1206:
527-550Crossref
(37)
Given
are
network,
undertake
several
adaptations
favor
synthesis
expense
decreasing
(Fig.
1).
Biochemical
approaches
highlight
unique
HSP
expression.
spatiotemporal
resolution
precise
now
being
uncovered
using
high-resolution
quantitative
microscopy.
Gene
adaptions
during
together
protect
macromolecules
promptly
cytoplasmic
nuclear
activities
once
permissive
restored
(3de
coordinates
other
protective
like
formation
RNP
integrated
(ISR)
repress
translation
initiation.
ISR
HSR
actions
endoplasmic
reticulum
(ER)
mitochondria
preserve
across
compartments.
ranging
plants
genes
encoding
HSPs.
grouped
families
based
on
apparent
weight
(18Jayaraj
G.G.
Hipp
M.S.
Hartl
F.U.
Functional
modules
network.Cold
Perspect.
12a033951Crossref
(47)
19Kampinga
H.H.
Hageman
J.
Vos
Kubota
Tanguay
R.M.
Bruford
E.A.
Cheetham
M.E.
Chen
Hightower
L.E.
Guidelines
nomenclature
human
proteins.Cell
Stress
Chaperones.
14:
105-111Crossref
(813)
HSP70
HSP90
functionally
relevant
(15Rosenzweig
20Abisambra
J.F.
Blair
L.J.
Hill
S.E.
Jones
J.R.
Kraft
Rogers
Koren
Jinwal
U.K.
Lawson
Johnson
A.G.
Wilcock
O'Leary
J.C.
Jansen-West
Muschol
Golde
T.E.
et
al.Phosphorylation
dynamics
regulate
Hsp27-mediated
rescue
neuronal
plasticity
deficits
tau
transgenic
mice.J.
Neurosci.
2010;
30:
15374-15382Crossref
(78)
They
ATP-dependent
cooperate
small
HSP110.
Cochaperones
J-domain
family
modulate
accelerating
ATP
hydrolysis,
participating
substrate
recognition
refolding
2)
(21Gamerdinger
Hajieva
Kaya
A.M.
Wolfrum
U.
Behl
Protein
involves
recruitment
macroautophagy
pathway
BAG3.EMBO
889-901Crossref
(385)
22Kumar
Ambasta
R.K.
Veereshwarayya
V.
Rosen
K.M.
Kosik
Band
Mestril
Patterson
Querfurth
H.W.
CHIP
interact
beta-APP
proteasome-dependent
manner
influence
Abeta
metabolism.Hum.
16:
848-864Crossref
23Lindquist
1986;
55:
1151-1191Crossref
24Lindquist
Craig
1988;
22:
631-677Crossref
25Liu
Liang
Zhou
Structural
analysis
Hsp70/Hsp40
system.Protein
Sci.
29:
378-390Crossref
(28)
26Petrucelli
Dickson
Kehoe
Taylor
Snyder
Grover
De
Lucia
McGowan
E.
Lewis
Prihar
Kim
Dillmann
W.H.
Browne
Hall
Voellmy
al.CHIP
ubiquitination,
aggregation.Hum.
2004;
13:
703-714Crossref
(560)
27Ritossa
puffing
pattern
induced
DNP
drosophila.Experientia.
1962;
18:
571-573Crossref
(1424)
further
categorized
constitutive
inducible
steady-state
levels.
some
upregulated
extent
upon
Among
them,
fastest
(23Lindquist
Interestingly,
highly
conserved
among
species
having
amino
acid
similarity
50%
Homo
sapiens
Escherichia
coli,
while
domains
96%
similar,
highlights
its
vital
adaption
changing
(28Sørensen
J.G.
Kristensen
T.N.
Loeschcke
ecological
proteins:
Heat
proteins.Ecol.
2003;
6:
1025-1037Crossref
Scholar).Figure
2The
HSC70/HSP70
retaining
proteostasis.
illustration
depicts
significant
tasks
network
inside
(Starting
top
left
tile)
Under
nonstress
HSC70
provides
cotranslational
polypeptide
obtain
conformation;
helps
proteins;
transports
cytoplasm
where
assisted
mitochondrial
(mtHSP70)
HSP60
attain
involved
complex
and/or
disassembly;
leads
lysosome
chaperone-mediated
autophagy
(236Massey
Kiffin
Cuervo
Pathophysiology
autophagy.Int.
36:
2420-2434Crossref
(148)
237Majeski
A.E.
Dice
Mechanisms
2435-2444Crossref
(299)
(Continuing
bottom
During
lack
exit
ribosome
tunnel
represses
elongation
stage.
resolves
granules
so
sequestered
mRNAs
recovery
stress;
targets
terminally
proteasomal
degradation;
autophagosome.
HSP,
protein.View
Large
Image
Figure
ViewerDownload
Hi-res
image
Download
(PPT)
frame
context
undertaken
eukaryotic
temperature.
We
compare
mounted
suggest
technological
overcome
gap
our
knowledge
one
main
Their
occurs
downregulation
constitutively
expressed
genes.
Most
short
(around
2500
nucleotides)
intronless,
promoter
contains
more
binding
sites,
elements
(HSEs),
association
master
factor
1
(HSF1)
(29Brocchieri
Conway
de
Macario
A.J.
hsp70
genome:
Conservation
differentiation
patterns
predict
wide
array
specialized
functions.BMC
Evol.
8:
19Crossref
(178)
not
expressed.
However,
loci
neither
present
compact
heterochromatin
domain
nor
marked
repressive
epigenetic
histone
modification.
3′
end
nucleosome-free
body
covered
nucleosomes.
bound
paused
polymerase
II
(RNAPII)
(30Petesch
S.J.
Lis
J.T.
Rapid,
transcription-independent
loss
nucleosomes
over
large
chromatin
loci.Cell.
134:
74-84Abstract
(250)
These
characteristics
stable
repression
facilitate
prompt
HSF1.
HSF1
shuttles
nucleus
cytoplasm,
kept
inactive
monomer
members
families.
released
trimerizes,
localizes
binds
HSE,
comprised
least
three
nGAAn
repeats
organized
head
tail
promoters
products
(31Anckar
Sistonen
Regulation
Implications
disease.Annu.
80:
1089-1115Crossref
(462)
32Vihervaara
glance.J.
127:
261-266Crossref
(169)
Scholar)
3).
domains,
oligomerization
next
N
terminus,
trans-activation
C
terminus
induces
initiation
elongation,
regulatory
middle
negatively
regulates
By
forming
trimer,
affinity
HSE
increases
each
trimer
repeat
domain.
sufficient
accompanied
extensive
modifications.
undergoes
hyperphosphorylation
serine
threonine
residues
cover
up
90%
(33Björk
J.K.
mammalian
family.FEBS
277:
4126-4139Crossref
34Gomez-Pastor
Burchfiel
E.T.
Thiele
D.J.
factors
roles
physiology
disease.Nat.
2018;
19:
4-19Crossref
(272)
35Guettouche
Boellmann
Lane
W.S.
Analysis
phosphorylation
experiencing
stress.BMC
4Crossref
(222)
36Nakai
HSF
regulation.Nat.
Struct.
93-95Crossref
(15)
only
few
serines
230
326,
necessary
(35Guettouche
37Boellmann
Guettouche
Fenna
Mnayer
DAXX
interacts
enhances
activity.Proc.
Natl.
Acad.
101:
4100-4105Crossref
(70)
Concomitantly,
sumo
groups
inhibitory
effect
removed
(38Hietakangas
Anckar
Blomster
H.A.
Fujimoto
Palvimo
J.J.
Nakai
PDSM,
motif
phosphorylation-dependent
SUMO
modification.Proc.
2006;
103:
45-50Crossref
(374)
acetylation
lysines
116
118
favors
activity,
whereas
lysine
localization
Acetylation
hours
after
decrease
(39Westerheide
S.D.
Stevens
S.M.
Stress-inducible
deacetylase
SIRT1.Science.
323:
1063-1066Crossref
(530)
summary,
regulated
under
various
stresses.
Although
modifications
identified,
many
others,
well
responsible
remains
elucidated.
combination
titration
demonstrated
Recent
work
yeast,
Saccharomyces
cerevisiae,
allowed
building
simple
mathematical
model
points
dissociation
HSP70/HSP90
first
"switch
on"
step
feedback
switch
off
(40Krakowiak
Zheng
X.
Patel
Feder
Z.A.
Anandhakumar
Valerius
Gross
D.S.
Khalil
A.S.
Pincus
Hsf1
constitute
two-component
loop
response.Elife.
7e31668Crossref
(33)
41Zheng
Krakowiak
Beyzavi
Ezike
Dynamic
phosphorylation.Elife.
5e18638Crossref
(97)
al.
(41Zheng
identified
sites
were
able
phosphorylations
no
but
instead
favoring
mediator
complex.
Additionally,
eEF1A
noncoding
HSR1
activating
form
nucleoprotein
stimulate
trimerization
(42Shamovsky
Ivannikov
Kandel
E.S.
Gershon
Nudler
RNA-mediated
cells.Nature.
440:
556-560Crossref
(271)
Following
shock,
recruits
multiple
cofactors
(43Chen
Yu
Yang
Temple
Harbinski
Gao
Wilson
Pagliarini
Identification
mixed
lineage
leukemia
1(MLL1)
coactivator
1(HSF1)
90
(HSP90)
inhibition.J.
Chem.
289:
18914-18927Abstract
44Jonkers
Getting
speed
II.Nat.
2015;
167-177Crossref
(468)
45Mason
P.B.
Cooperative
competitive
interactions
promoter.J.
1997;
272:
33227-33233Abstract
46Park
J.M.
Werner
Y.J.
Mediator,
holoenzyme,
directly
recruited
shock.Mol.
2001;
9-19Abstract
(113)
Scholar),
SGO2,
subunit
MED12,
essential
strong
(47Takii
Matsumoto
Srivastava
Katiyar
Nakayama
K.I.
pericentromeric
shugoshin
2
cooperates
Pol
recruitment.EMBO
38e102566Crossref
(11)
SGO2
hypophosphorylated
RNAPII
Transcription
then
P-TEFb,
mediated
(48Lis
Mason
Peng
Price
D.H.
P-TEFb
kinase
loci.Genes
792-803Crossref
induce
C-terminal
RNAPII,
49Marshall
N.F.
Xie
Z.
Control
potential
novel
Carboxyl-terminal
kinase∗.J.
1996;
271:
27176-27183Abstract
positioned
along
removed.
remodelers
SWI/SNF
FACT
Spt6
Drosophila
melanogaster
(D.
melanogaster)
within
minutes
remove
Besides
HSF1,
depends
relocation
membrane
speckles
(50Khanna
Hu
Belmont
transgene
directed
motion
facilitates
activation.Curr.
24:
1138-1144Abstract
(85)
51Vera
Singer
regulation:
jumps
shocked.Curr.
R396-R398Abstract
rapid,
active,
unidirectional
movement
actin
polymerization.
locus
sequence
determines
contain
2–phosphorylated
components
machinery,
speckle
yet
identified.
coalesce
discrete
spots
stimulation.
interallelic
clustering
interaction
HSP104
HSP12
transcription.
suggested
presence
factories
formed
could
coregulated
(52Chowdhary
Kainth
undergo
alteration
three-dimensional
structure
genome
organization
stress.Mol.
37e00292-17Crossref
(17)
upregulation
non-HSP
cytoskeleton
oxidative
massive
thousands
(For
review:
(53Vihervaara
Duarte
F.M.
driving
responses.Nat.
385-397Crossref
(98)
Scholar)).
Detailed
position
polymerases,
landscape
explain
preferences
(54Mueller
Mieczkowski
Kundu
Wang
Sadreyev
Tolstorukov
M.Y.
Kingston
R.E.
Widespread
nucleosome
accessibility
without
occupancy
induction.Genes
31:
451-462Crossref
(55)
55Vihervaara
Mahat
D.B.
Guertin
Chu
Danko
C.G.
Transcriptional
pre-wired
enhancer
architecture.Nat.
Commun.
255Crossref
(65)
does
remodeling
topology
associated
S2
(56Ray
Munn
P.R.
Vihervaara
Ozer
Chromatin
conformation
cha
Язык: Английский
Tissue-specific landscape of protein aggregation and quality control in an aging vertebrate
Developmental Cell,
Год журнала:
2024,
Номер
59(14), С. 1892 - 1911.e13
Опубликована: Май 28, 2024
Язык: Английский
Pathology in Parkinson’s Disease
Cambridge University Press eBooks,
Год журнала:
2025,
Номер
unknown, С. 194 - 201
Опубликована: Янв. 7, 2025
Язык: Английский
Adapting the proteostasis capacity to sustain brain healthspan
Cell,
Год журнала:
2021,
Номер
184(6), С. 1545 - 1560
Опубликована: Март 1, 2021
Язык: Английский
Asynchronous, contagious and digital aging
Nature Aging,
Год журнала:
2021,
Номер
1(1), С. 29 - 35
Опубликована: Янв. 14, 2021
Язык: Английский
Modulation of Amyloid States by Molecular Chaperones
Cold Spring Harbor Perspectives in Biology,
Год журнала:
2019,
Номер
11(7), С. a033969 - a033969
Опубликована: Фев. 12, 2019
Anne
Wentink,
Carmen
Nussbaum-Krammer
and
Bernd
Bukau
Center
for
Molecular
Biology
of
Heidelberg
University
(ZMBH)
German
Cancer
Research
(DKFZ),
DKFZ-ZMBH
Alliance,
D-69120
Heidelberg,
Germany
Correspondence:
bukau{at}zmbh.uni-heidelberg.de
Язык: Английский
