SUMOylation in development and neurodegeneration | Zendy

Tak-Yu Yau | Zendy; Òscar Molina | Zendy; Albert J. Courey | Zendy

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SUMOylation in development and neurodegeneration

Author(s) -

Tak-Yu Yau,

Òscar Molina,

Albert J. Courey

Publication year - 2020

Publication title -

development

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.754

H-Index - 325

eISSN - 1477-9129

pISSN - 0950-1991

DOI - 10.1242/dev.175703

Subject(s) - sumo protein , biology , neurodegeneration , neurogenesis , ubiquitin , microbiology and biotechnology , transcription factor , epigenetics , signal transduction , lysine , neuroscience , genetics , disease , gene , medicine , pathology , amino acid

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.

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