Cyclin Y, a novel actin-binding protein, regulates spine plasticity through the cofilin-actin pathway

Hongik Hwang, Young Na Hur, Heesung Sohn, Jiyeon Seo, Jung Hwa Hong, Eunsil Cho, Yuri Choi, Saebom Lee, Seongeun Song, A. Ram Lee, Suyeon Kim, Dong Gyu Jo, Hyewhon Rhim, Mikyoung Park

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


While positive regulators of hippocampal long-term potentiation (LTP) have extensively been investigated, relatively little is known about the inhibitory regulators of LTP. We previously reported that Cyclin Y (CCNY), a member of cyclin family generally known to function in proliferating cells, is a novel postsynaptic protein that serves as a negative regulator of functional LTP. However, whether CCNY plays a role in structural LTP, which is mechanistically linked to functional LTP, and which mechanisms are involved in the CCNY-mediated suppression of LTP at the molecular level remain elusive. Here, we report that CCNY negatively regulates the plasticity-induced changes in spine morphology through the control of actin dynamics. We observed that CCNY directly binds to filamentous actin and interferes with LTP-induced actin polymerization as well as depolymerization by blocking the activation of cofilin, an actin-depolymerizing factor, thus resulting in less plastic spines and the impairment of structural LTP. These data suggest that CCNY acts as an inhibitory regulator for both structural and functional LTP by modulating actin dynamics through the cofilin-actin pathway. Collectively, our findings provide a mechanistic insight into the inhibitory modulation of hippocampal LTP by CCNY, highlighting a novel function of a cyclin family protein in non-proliferating neuronal cells.

Original languageEnglish
Article number101915
JournalProgress in Neurobiology
StatePublished - Mar 2021


  • Actin
  • Cofilin
  • Cyclin Y
  • Spine plasticity
  • Structural long-term potentiation


Dive into the research topics of 'Cyclin Y, a novel actin-binding protein, regulates spine plasticity through the cofilin-actin pathway'. Together they form a unique fingerprint.

Cite this