Journal
LIFE-BASEL
Volume 11, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/life11111132
Keywords
neuron; synapse; dendritic spine; actin cytoskeleton; GTPase; post-translational modification
Categories
Funding
- Research Grant Council of Hong Kong [17106018, 17117720]
- Area of Excellence Scheme [AoE/M-604/16]
- Theme-based Research Scheme [T13-605/18-W]
- University Grants Committee of Hong Kong
- Health and Medical Research Fund [06172986]
- Food and Health Bureau of the Hong Kong SAR Government
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PRMT8, among the nine mammalian protein arginine methyltransferases, stands out for its restricted expression in the nervous system and being the only membrane-bound PRMT. Studies have shown its involvement in various neuronal functions such as dendritic growth, synapse maturation, and synaptic plasticity. There is also emerging evidence suggesting a potential role of PRMT8 in neurological diseases.
Among the nine mammalian protein arginine methyltransferases (PRMTs), PRMT8 is unusual because it has restricted expression in the nervous system and is the only membrane-bound PRMT. Emerging studies have demonstrated that this enzyme plays multifaceted roles in diverse processes in neurons. Here we will summarize the unique structural features of PRMT8 and describe how it participates in various neuronal functions such as dendritic growth, synapse maturation, and synaptic plasticity. Recent evidence suggesting the potential role of PRMT8 function in neurological diseases will also be discussed.
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