Emerging roles of Lys63-linked polyubiquitination in neuronal excitatory postsynapses
- Authors
- Kim, Shinhyun; Zhang, Yinhua; Jin, Chunmei; Lee, Yeunkum; Kim, Yoonhee; Han, Kihoon
- Issue Date
- Apr-2019
- Publisher
- PHARMACEUTICAL SOC KOREA
- Keywords
- Lys63-linked polyubiquitination; Excitatory postsynapse; Postsynaptic density; CYLD; PSD-95
- Citation
- ARCHIVES OF PHARMACAL RESEARCH, v.42, no.4, pp.285 - 292
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- ARCHIVES OF PHARMACAL RESEARCH
- Volume
- 42
- Number
- 4
- Start Page
- 285
- End Page
- 292
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/66541
- DOI
- 10.1007/s12272-018-1081-8
- ISSN
- 0253-6269
- Abstract
- In the mammalian brain, neuronal excitatory synaptic development, function, and plasticity largely rely on dynamic, activity-dependent changes in the macromolecular protein complex called the postsynaptic density (PSD). Activity-dependent Lys48-linked polyubiquitination and subsequent proteasomal degradation of key proteins in the PSD have been reported. However, investigations into the functions and regulatory mechanisms of Lys63-linked polyubiquitination, the second most abundant polyubiquitin form in synapses, have recently begun. Recent studies showed that a Lys63 linkage-specific deubiquitinase (DUB), cylindromatosis-associated DUB (CYLD) localizes to the PSD where its DUB activity is regulated by different kinases. In addition, Lys63-linked polyubiquitination of postsynaptic density 95 (PSD-95), a core scaffolding protein of the PSD, was identified and its functional significance in synaptic plasticity was characterized. In this review, we summarize these recent findings on Lys63-linked polyubiquitination in excitatory postsynapses, and also propose key questions and prospects about this emerging type of posttranslational modification of the PSD proteome.
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