The G3BP1 RNP complex at focal adhesion tunes cell migration

Zhiying Yao; Ziqiu Wang; Peiguo Yang

doi:10.1016/j.tcb.2025.02.001

The G3BP1 RNP complex at focal adhesion tunes cell migration

Trends Cell Biol. 2025 Mar;35(3):180-182. doi: 10.1016/j.tcb.2025.02.001. Epub 2025 Feb 20.

Authors

Zhiying Yao¹, Ziqiu Wang¹, Peiguo Yang²

Affiliations

¹ School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China; Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
² School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China; Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China. Electronic address: yangpeiguo@westlake.edu.cn.

PMID: 39984361
DOI: 10.1016/j.tcb.2025.02.001

Abstract

Ribonucleoprotein (RNP) complexes can form multiple mesoscale assemblies, including stress granules (SGs). However, the function and regulation of the soluble RNP complexes are not fully understood. A recent study by Boraas et al. showed that G3BP1, a key node in SG formation, forms focal adhesion (FA)-localized RNP complexes and regulates cell migration.

MeSH terms

Animals
Cell Movement*
DNA Helicases* / metabolism
Focal Adhesions* / metabolism
Humans
Poly-ADP-Ribose Binding Proteins* / metabolism
RNA Helicases* / metabolism
RNA Recognition Motif Proteins* / metabolism
Ribonucleoproteins* / metabolism
Stress Granules / metabolism

Substances

Ribonucleoproteins
RNA Recognition Motif Proteins
RNA Helicases
G3BP1 protein, human
Poly-ADP-Ribose Binding Proteins
DNA Helicases