SUMOylation in development and neurodegeneration.
Epigenetics
Neurodegenerative disorder
Post-translational protein modification
SUMO
Signal transduction
Ubiquitin-like protein
Journal
Development (Cambridge, England)
ISSN: 1477-9129
Titre abrégé: Development
Pays: England
ID NLM: 8701744
Informations de publication
Date de publication:
18 03 2020
18 03 2020
Historique:
entrez:
20
3
2020
pubmed:
20
3
2020
medline:
29
10
2020
Statut:
epublish
Résumé
In essentially all eukaryotes, proteins can be modified by the attachment of small ubiquitin-related modifier (SUMO) proteins to lysine side chains to produce branched proteins. This process of 'SUMOylation' plays essential roles in plant and animal development by altering protein function in spatially and temporally controlled ways. In this Primer, we explain the process of SUMOylation and summarize how SUMOylation regulates a number of signal transduction pathways. Next, we discuss multiple roles of SUMOylation in the epigenetic control of transcription. In addition, we evaluate the role of SUMOylation in the etiology of neurodegenerative disorders, focusing on Parkinson's disease and cerebral ischemia. Finally, we discuss the possibility that SUMOylation may stimulate survival and neurogenesis of neuronal stem cells.
Identifiants
pubmed: 32188601
pii: 147/6/dev175703
doi: 10.1242/dev.175703
pmc: PMC7097199
pii:
doi:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM063596
Pays : United States
Organisme : NIMH NIH HHS
ID : R21 MH119020
Pays : United States
Organisme : NIGMS NIH HHS
ID : T34 GM008563
Pays : United States
Informations de copyright
© 2020. Published by The Company of Biologists Ltd.
Déclaration de conflit d'intérêts
Competing interestsThe authors declare no competing or financial interests.
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