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SUMOylation in development and neurodegeneration

Tak-Yu Yau, Òscar Molina, Albert J. Courey

2020Development58 citationsDOIOpen Access PDF

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.

Topics & Concepts

SUMO proteinBiologyNeurodegenerationNeurogenesisUbiquitinCell biologyTranscription factorEpigeneticsSignal transductionLysineNeuroscienceGeneticsDiseaseGeneMedicinePathologyAmino acidUbiquitin and proteasome pathwaysGlycosylation and Glycoproteins ResearchGenetics and Neurodevelopmental Disorders
SUMOylation in development and neurodegeneration | Litcius