Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 112, Issue -, Pages -Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.mcn.2021.103602
Keywords
Ubiquitin; E3 ligase; Synapse; Neuron
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Funding
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [368482240/GRK2416, STE1117/10-1]
- JSPS KAKENHI [JP20K07334]
- Ohsumi Frontier Science Foundation
- Takeda Science Foundation
- Uehara Memorial Foundation
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Ubiquitination is crucial for the regulation of synaptogenesis and synaptic transmission, with abnormalities in E3 genes leading to neurodegenerative disorders and impairing synapse function.
Ubiquitination is a key posttranslational modification for the controlled protein degradation and proteostasis. The substrate specificity is determined by a family of E3 ubiquitin ligases, which are encoded by more than 600 genes in the mammalian genome. Gain- or loss-of-function of a number of E3 genes results in neurodegeneration or neurodevelopmental disorders, affecting synapse function. This implies that the specific ubiquitination of synaptic substrates are of crucial importance for the normal neuronal network. In this review, we will summarize the history, current topics, and challenges in the field of ubiquitination-dependent regulations of synaptogenesis and synaptic transmission.
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