NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3

Hsu Wen Chao, Yen Ting Lai, Yi Ling Lu, Chi Long Lin, Wei Mai, Yi Shuian Huang

研究成果: 雜誌貢獻文章同行評審

40 引文 斯高帕斯(Scopus)


Cytoplasmic polyadenylation element-binding protein (CPEB)3 is a nucleocytoplasm-shuttling RNA-binding protein and predominantly resides in the cytoplasm where it represses target RNA translation. When translocated into the nucleus, CPEB3 binds to Stat5b and downregulates Stat5b-dependent transcription. In neurons, the activation of N-methyl-d-aspartate receptors (NMDARs) accumulates CPEB3 in the nucleus and redistributes CPEB3 in the nucleocytoplasmic compartments to control gene expression. Nonetheless, it is unclear which karyopherin drives the nuclear import of CPEB3 and which transport direction is most affected by NMDA stimulation to increase the nuclear pool of CPEB3. Here, we have identified that the karyopherins, IPO5 and CRM1, facilitate CPEB3 translocation by binding to RRM1 and a leucine-containing motif of CPEB3, respectively. NMDAR signaling increases RanBP1 expression and reduces the level of cytoplasmic GTP-bound Ran. These changes enhance CPEB3-IPO5 interaction, which consequently accelerates the nuclear import of CPEB3. This study uncovers a novel NMDA-regulated import pathway to facilitate the nuclear translocation of CPEB3.
頁(從 - 到)8484-8498
期刊Nucleic Acids Research
出版狀態已發佈 - 9月 2012

ASJC Scopus subject areas

  • 遺傳學


深入研究「NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3」主題。共同形成了獨特的指紋。