| Literature DB >> 32188601 |
Tak-Yu Yau1, Oscar Molina1, Albert J Courey2.
Abstract
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.Entities:
Keywords: Epigenetics; Neurodegenerative disorder; Post-translational protein modification; SUMO; Signal transduction; Ubiquitin-like protein
Mesh:
Year: 2020 PMID: 32188601 PMCID: PMC7097199 DOI: 10.1242/dev.175703
Source DB: PubMed Journal: Development ISSN: 0950-1991 Impact factor: 6.862