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<p>Cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is an RNA-binding protein that plays a pivotal role in the formation of long-term memory. The N-terminal region (residues 1–459) of CPEB3 is a highly aggregative intrinsically disordered region (IDR) that regulates the translation of specific targets, such as AMPA subunits, through mechanisms including liquid-liquid phase separation (LLPS) and the formation of fibrous aggregates. Despite its significance, the underlying mechanisms remain poorly understood. In this study, we present the backbone resonance assignments of residues 101–200 and 294–410 segments of the CPEB3 IDR. In agreement with sequence-based predictions, CPEB3 [101–200] was found to be disordered, whereas two partial α-helices were identified within CPEB3 [294–410].</p>

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Backbone resonance assignments of the CPEB3 [101–200] and CPEB3 [294–410]

  • 期刊论文

  • 发表日期：

    2025年3月29日

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  • Harunobu Saito,
  • Yujin Lee,
  • Motoharu Ueno,
  • Naotaka Sekiyama,
  • Masatomo So,
  • Ayako Furukawa,
  • Kenji Sugase

摘要

Cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is an RNA-binding protein that plays a pivotal role in the formation of long-term memory. The N-terminal region (residues 1–459) of CPEB3 is a highly aggregative intrinsically disordered region (IDR) that regulates the translation of specific targets, such as AMPA subunits, through mechanisms including liquid-liquid phase separation (LLPS) and the formation of fibrous aggregates. Despite its significance, the underlying mechanisms remain poorly understood. In this study, we present the backbone resonance assignments of residues 101–200 and 294–410 segments of the CPEB3 IDR. In agreement with sequence-based predictions, CPEB3 [101–200] was found to be disordered, whereas two partial α-helices were identified within CPEB3 [294–410].