|
KMID : 0043320190420040285
|
|
Archives of Pharmacal Research
2019 Volume.42 No. 4 p.285 ~ p.292
|
|
|
Emerging roles of Lys63-linked polyubiquitination in neuronal excitatory postsynapses
|
|
Kim Shin-Hyun
Zhang Yinhua
Jin Chunmei
Lee Yeun-Kum
Kim Yoon-Hee
Han Ki-Hoon
|
|
|
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.
|
|
|
KEYWORD
|
|
|
Lys63-linked polyubiquitination, Excitatory postsynapse, Postsynaptic density, CYLD, PSD-95
|
|
|
FullTexts / Linksout information
|
|
|
|
|
Listed journal information
|
|
  
|
|