Neuroscience Bulletin

, Volume 34, Issue 6, pp 1100–1102 | Cite as

SUMOylation of Fragile X Mental Retardation Protein: A Critical Mechanism of FMRP-Mediated Neuronal Function

  • Mingzhu Tang
  • Liqun Lu
  • Feng XieEmail author
  • Linxi ChenEmail author
Research Highlight

Recently, Khayachi et al. [1] showed that fragile X mental retardation protein (FMRP) is an active substrate of the small ubiquitin-like modifier (SUMO) pathway in neurons. FMRP SUMOylation is induced by the activation of metabotropic glutamate receptors (mGlu5Rs). FMRP SUMOylation is required for dissociating FMRP from dendritic RNA granules and controlling spine density and proper maturation. Mechanically, the SUMOylation process is triggered by the activation of mGlu5Rs, thereby contributing to maintaining FMRP-mediated neuronal function. In fact, some proteins that mediate synaptic plasticity, neurotransmitter release, and neuronal network formation [2, 3, 4], are mostly regulated by SUMOylation. Therefore, SUMOylation has emerged as an essential posttranslational modification in the nervous system. This novel discovery first provides evidence to support the idea that FMRP is a novel substrate of SUMOylation and acts as an essential regulator in the developing brain. Clearly, it...



This highlight was supported by the National Natural Science Foundation of China (81503074).

Compliance with Ethical Standards

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Shanghai Institutes for Biological Sciences, CAS and Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  1. 1.Institute of Pharmacy and Pharmacology, Learning Key Laboratory for Pharmacoproteomics, Hunan Province Cooperative Innovation Center for Molecular Target New Drug StudyUniversity of South ChinaHengyangChina

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