Your browser doesn't support javascript.
loading
Yin and yang regulation of stress granules by Caprin-1.
Song, Dan; Kuang, Lisha; Yang, Lin; Wang, Lei; Li, Hao; Li, Xiu; Zhu, Zhimin; Shi, Chaowei; Zhu, Haining; Gong, Weimin.
Afiliación
  • Song D; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
  • Kuang L; Department of Pharmacology and Toxicology, R. Ken Coit College of Pharmacy, University of Arizona, Tucson, AZ 85721.
  • Yang L; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
  • Wang L; Department of Pharmacology and Toxicology, R. Ken Coit College of Pharmacy, University of Arizona, Tucson, AZ 85721.
  • Li H; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
  • Li X; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
  • Zhu Z; Institute of Applied Physics, Chinese Academy of Sciences, 201899 Shanghai, China.
  • Shi C; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
  • Zhu H; Department of Pharmacology and Toxicology, R. Ken Coit College of Pharmacy, University of Arizona, Tucson, AZ 85721.
  • Gong W; School of Life Sciences, University of Science and Technology of China, Hefei, 230027 China.
Proc Natl Acad Sci U S A ; 119(44): e2207975119, 2022 11.
Article en En | MEDLINE | ID: mdl-36279435
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.
Asunto(s)
Palabras clave

Texto completo: 1 Bases de datos: MEDLINE Medicinas Tradicionales: Medicinas_tradicionales_de_asia / Medicina_china Asunto principal: ADN Helicasas / ARN Helicasas Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2022 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Medicinas Tradicionales: Medicinas_tradicionales_de_asia / Medicina_china Asunto principal: ADN Helicasas / ARN Helicasas Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2022 Tipo del documento: Article