Yin and yang regulation of stress granules by Caprin-1

Dan Song, Lisha Kuang, Lin Yang, Lei Wang, Hao Li, Xiu Li, Zhimin Zhu, Chaowei Shi, Haining Zhu, Weimin Gong

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Stress granules (SGs) are cytoplasmic biomolecular condensates containing proteins and RNAs in response to stress. Ras-GTPase–activating protein binding protein 1 (G3BP1) is a core SG protein. Caprin-1 and ubiquitin specific peptidase 10 (USP10) interact with G3BP1, facilitating and suppressing SG formation, respectively. The crystal structures of the nuclear transport factor 2-like (NTF2L) domain of G3BP1 in complex with the G3BP1-interacting motif (GIM) of Caprin-1 and USP10 show that both GIMs bind to the same hydrophobic pocket of G3BP1. Moreover, both GIMs suppressed the liquid–liquid phase separation (LLPS) of G3BP1, suggesting that Caprin-1 likely facilitates SG formation via other mechanisms. Thus, we dissected various domains of Caprin-1 and investigated their role in LLPS in vitro and SG formation in cells. The C-terminal domain of Caprin-1 underwent spontaneous LLPS, whereas the N-terminal domain and GIM of Caprin-1 suppressed LLPS of G3BP1. The opposing effect of the N- and C-terminal domains of Caprin-1 on SG formation were demonstrated in cells with or without the endogenous Caprin-1. We propose that the N- and C-terminal domains of Caprin-1 regulate SG formation in a “yin and yang” fashion, mediating the dynamic and reversible assembly of SGs.

Original languageEnglish (US)
Article numbere2207975119
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number44
StatePublished - Nov 1 2022


  • Caprin-1
  • G3BP1
  • RNA-binding proteins
  • liquid–liquid phase separation
  • stress granules

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Yin and yang regulation of stress granules by Caprin-1'. Together they form a unique fingerprint.

Cite this