G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration

• DOI: 10.1016/j.celrep.2025.115237
• Publication Date: 2025-02-01T06:53:35Z
• Authors: Liana C. Boraas; Mengwei Hu; Pieter Martino; Lauren Thornton; Charles E. Vejnar; Gang Zhen; Longhui Zeng; Dylan M. Parker; Andy L. Cox; Antonio J. Giraldez; Xiaolei Su; Christine Mayr; Siyuan Wang; Stefania Nicoli
• Keywords: Stress granule; Messenger RNP; Poly(N-isopropylacrylamide)

The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration. For instance, β-actin mRNA and its associated RNA-binding protein (RBP), ZBP1/IGF2BP1, are recruited to focal adhesions (FAs) support localized synthesis, crucial for However, whether other RBPs also localize at FAs remains unclear. Here, we identify hundreds that enriched (FA-mRNAs). FA-mRNAs share characteristics with stress granule (SG) found ribonucleoprotein (RNP) complexes the SG RBP. Mechanistically, G3BP1 binds FA proteins an RNA-dependent manner, dimerization domains, essential form RNPs SG, required We find promote speed by enhancing mobility size. These findings suggest previously unappreciated regulating function under non-stress conditions.