Post-translational modifications: Regulators of neurodegenerative proteinopathies

Post-translational modifications (PTMs) are divided into four groups based on the type of modifications such as the addition of chemical groups (methylation, acetylation, formylation, carboxylation), the addition of polypeptides (ubiquitination, SUMOylation, neddylation), amino acid and structural c...

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Published inAgeing research reviews Vol. 68; p. 101336
Main Authors Gupta, Rohan, Sahu, Mehar, Srivastava, Devesh, Tiwari, Swati, Ambasta, Rashmi K., Kumar, Pravir
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 01.07.2021
Subjects
Cellular signaling
Neurodegenerative disease
Post-translational modifications
Protein aggregation
Proteinopathies
Unfolded protein response
DNMTs
APP
NF-κβ
PAD4
UBE2D2
PI3K
CMA
UPR
UPS
CHOP
PDK1
RRMs
AD
SREBP
TET-1
DYRK1A
β-TrCP
DKK1
PDR1
AMPK
ULK1
VDAC1
ERK
HDAC
TCF/LEF
UCH-L1
PSEN2
CNS
ATFS1
PSEN1
LRP5/6
FOXO1
HSPs
LAMP2A
Unfolded protein response
GSK-3β
NLS
TAK1
ATF6α
CSMNs
COX2
polyQ
GADD34
ACC
XBP1
Cellular signaling
FUS
DR5
PLK2
IKK
PARP16
DJ1
AGEs
PGC-1α
Umf1
RAGE
NFTs
CDK5
SP2
SP1
TM
Prx2
REP
NES
ATP
Proteinopathies
PAR
Protein aggregation
E-2609
LRRK2
PPIase
ALS
MTS
ADP
DLP-1
Aβ
Dsh
iNOS
PH domain
AMP
PKA
ASK1-JNK
SNpc
TRAF2
IGF-1
MAPK
CaMKKβ
NGF
IT15
ER
ERAD
BACE1
PARKIN
TSC 1/2
TDP-43
TRAF6
Cdks
ROS
PIP3
LBs
mTORC2
mTORC1
PIP2
elF2α
NDDs
NO
USP14
3-NPA
BCL-xL
CK1
BiP
PERK
ACAT
SNX33
LKB1
Drp1
BCL-2
PDI
CBS
Neurodegenerative disease
AVs
ASK1
FTLD
htt
PTMs
SOD1
PIA2
NAD
PINK1
Post-translational modifications
PD
APC
NEDD4
IRE1α
HD
TARDBP
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Abstract Post-translational modifications (PTMs) are divided into four groups based on the type of modifications such as the addition of chemical groups (methylation, acetylation, formylation, carboxylation), the addition of polypeptides (ubiquitination, SUMOylation, neddylation), amino acid and structural changes (racemization, citrullination, Isoaspartate), and addition of complex molecules (palmitoylation, glypiation, oxidation, carbonylation). PTMs cause aggregation of misfolded proteins, which further causes an alteration in endoplasmic stress and unfolded protein response. This will deregulate cell-signaling cascades such as PI3K/Akt/GSK3β pathway, p38/MAPK pathway, Wnt signaling cascade, and AMPK transduction pathway. Further, deregulation in the cell-signaling cascade causes impairment in cellular processes such as autophagic degradation, mitochondrial dysfunction, inflammatory response, and cell-cycle deregulation, which increases neurotoxicity and, thus, neuronal cell death. [Display omitted] •Alteration in the protein quality control system causes protein dyshomeostasis.•Accumulation of non-functional protein is the main factor for neurodegenerative disorders (NDDs).•Post-translational modification (PTMs) can also help in the rescue of non-functional proteins.•Different PTMs enzymes serve as a therapeutic target in NDDs and reverse neurological defects. One of the hallmark features in the neurodegenerative disorders (NDDs) is the accumulation of aggregated and/or non-functional protein in the cellular milieu. Post-translational modifications (PTMs) are an essential regulator of non-functional protein aggregation in the pathogenesis of NDDs. Any alteration in the post-translational mechanism and the protein quality control system, for instance, molecular chaperone, ubiquitin-proteasome system, autophagy-lysosomal degradation pathway, enhances the accumulation of misfolded protein, which causes neuronal dysfunction. Post-translational modification plays many roles in protein turnover rate, accumulation of aggregate and can also help in the degradation of disease-causing toxic metabolites. PTMs such as acetylation, glycosylation, phosphorylation, ubiquitination, palmitoylation, SUMOylation, nitration, oxidation, and many others regulate protein homeostasis, which includes protein structure, functions and aggregation propensity. Different studies demonstrated the involvement of PTMs in the regulation of signaling cascades such as PI3K/Akt/GSK3β, MAPK cascade, AMPK pathway, and Wnt signaling pathway in the pathogenesis of NDDs. Further, mounting evidence suggests that targeting different PTMs with small chemical molecules, which acts as an inhibitor or activator, reverse misfolded protein accumulation and thus enhances the neuroprotection. Herein, we briefly discuss the protein aggregation and various domain structures of different proteins involved in the NDDs, indicating critical amino acid residues where PTMs occur. We also describe the implementation and involvement of various PTMs on signaling cascade and cellular processes in NDDs. Lastly, we implement our current understanding of the therapeutic importance of PTMs in neurodegeneration, along with emerging techniques targeting various PTMs.
AbstractList Post-translational modifications (PTMs) are divided into four groups based on the type of modifications such as the addition of chemical groups (methylation, acetylation, formylation, carboxylation), the addition of polypeptides (ubiquitination, SUMOylation, neddylation), amino acid and structural changes (racemization, citrullination, Isoaspartate), and addition of complex molecules (palmitoylation, glypiation, oxidation, carbonylation). PTMs cause aggregation of misfolded proteins, which further causes an alteration in endoplasmic stress and unfolded protein response. This will deregulate cell-signaling cascades such as PI3K/Akt/GSK3β pathway, p38/MAPK pathway, Wnt signaling cascade, and AMPK transduction pathway. Further, deregulation in the cell-signaling cascade causes impairment in cellular processes such as autophagic degradation, mitochondrial dysfunction, inflammatory response, and cell-cycle deregulation, which increases neurotoxicity and, thus, neuronal cell death. [Display omitted] •Alteration in the protein quality control system causes protein dyshomeostasis.•Accumulation of non-functional protein is the main factor for neurodegenerative disorders (NDDs).•Post-translational modification (PTMs) can also help in the rescue of non-functional proteins.•Different PTMs enzymes serve as a therapeutic target in NDDs and reverse neurological defects. One of the hallmark features in the neurodegenerative disorders (NDDs) is the accumulation of aggregated and/or non-functional protein in the cellular milieu. Post-translational modifications (PTMs) are an essential regulator of non-functional protein aggregation in the pathogenesis of NDDs. Any alteration in the post-translational mechanism and the protein quality control system, for instance, molecular chaperone, ubiquitin-proteasome system, autophagy-lysosomal degradation pathway, enhances the accumulation of misfolded protein, which causes neuronal dysfunction. Post-translational modification plays many roles in protein turnover rate, accumulation of aggregate and can also help in the degradation of disease-causing toxic metabolites. PTMs such as acetylation, glycosylation, phosphorylation, ubiquitination, palmitoylation, SUMOylation, nitration, oxidation, and many others regulate protein homeostasis, which includes protein structure, functions and aggregation propensity. Different studies demonstrated the involvement of PTMs in the regulation of signaling cascades such as PI3K/Akt/GSK3β, MAPK cascade, AMPK pathway, and Wnt signaling pathway in the pathogenesis of NDDs. Further, mounting evidence suggests that targeting different PTMs with small chemical molecules, which acts as an inhibitor or activator, reverse misfolded protein accumulation and thus enhances the neuroprotection. Herein, we briefly discuss the protein aggregation and various domain structures of different proteins involved in the NDDs, indicating critical amino acid residues where PTMs occur. We also describe the implementation and involvement of various PTMs on signaling cascade and cellular processes in NDDs. Lastly, we implement our current understanding of the therapeutic importance of PTMs in neurodegeneration, along with emerging techniques targeting various PTMs.
One of the hallmark features in the neurodegenerative disorders (NDDs) is the accumulation of aggregated and/or non-functional protein in the cellular milieu. Post-translational modifications (PTMs) are an essential regulator of non-functional protein aggregation in the pathogenesis of NDDs. Any alteration in the post-translational mechanism and the protein quality control system, for instance, molecular chaperone, ubiquitin-proteasome system, autophagy-lysosomal degradation pathway, enhances the accumulation of misfolded protein, which causes neuronal dysfunction. Post-translational modification plays many roles in protein turnover rate, accumulation of aggregate and can also help in the degradation of disease-causing toxic metabolites. PTMs such as acetylation, glycosylation, phosphorylation, ubiquitination, palmitoylation, SUMOylation, nitration, oxidation, and many others regulate protein homeostasis, which includes protein structure, functions and aggregation propensity. Different studies demonstrated the involvement of PTMs in the regulation of signaling cascades such as PI3K/Akt/GSK3β, MAPK cascade, AMPK pathway, and Wnt signaling pathway in the pathogenesis of NDDs. Further, mounting evidence suggests that targeting different PTMs with small chemical molecules, which acts as an inhibitor or activator, reverse misfolded protein accumulation and thus enhances the neuroprotection. Herein, we briefly discuss the protein aggregation and various domain structures of different proteins involved in the NDDs, indicating critical amino acid residues where PTMs occur. We also describe the implementation and involvement of various PTMs on signaling cascade and cellular processes in NDDs. Lastly, we implement our current understanding of the therapeutic importance of PTMs in neurodegeneration, along with emerging techniques targeting various PTMs.
ArticleNumber 101336
Author Gupta, Rohan
Sahu, Mehar
Srivastava, Devesh
Tiwari, Swati
Kumar, Pravir
Ambasta, Rashmi K.
Author_xml – sequence: 1
  givenname: Rohan
  surname: Gupta
  fullname: Gupta, Rohan
– sequence: 2
  givenname: Mehar
  surname: Sahu
  fullname: Sahu, Mehar
– sequence: 3
  givenname: Devesh
  surname: Srivastava
  fullname: Srivastava, Devesh
– sequence: 4
  givenname: Swati
  surname: Tiwari
  fullname: Tiwari, Swati
– sequence: 5
  givenname: Rashmi K.
  orcidid: 0000-0002-8874-7752
  surname: Ambasta
  fullname: Ambasta, Rashmi K.
– sequence: 6
  givenname: Pravir
  orcidid: 0000-0001-7444-2344
  surname: Kumar
  fullname: Kumar, Pravir
  email: pravirkumar@dtu.ac.in
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33775891$$D View this record in MEDLINE/PubMed
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ATP
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PPIase
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MTS
ADP
DLP-1
Aβ
Dsh
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PH domain
AMP
PKA
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SNpc
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IGF-1
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FTLD
htt
PTMs
SOD1
PIA2
NAD
PINK1
Post-translational modifications
PD
APC
NEDD4
IRE1α
HD
TARDBP
Language English
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PublicationTitle Ageing research reviews
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Snippet Post-translational modifications (PTMs) are divided into four groups based on the type of modifications such as the addition of chemical groups (methylation,...
One of the hallmark features in the neurodegenerative disorders (NDDs) is the accumulation of aggregated and/or non-functional protein in the cellular milieu....
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SubjectTerms Cellular signaling
Neurodegenerative disease
Post-translational modifications
Protein aggregation
Proteinopathies
Unfolded protein response
Title Post-translational modifications: Regulators of neurodegenerative proteinopathies
URI https://dx.doi.org/10.1016/j.arr.2021.101336
https://www.ncbi.nlm.nih.gov/pubmed/33775891
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