Related Experiment Video

Updated: May 30, 2025

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

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G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration

Liana C Boraas1, Mengwei Hu2, Pieter Martino1

  • 1Yale Cardiovascular Research Center, Department of Internal Medicine, Section of Cardiology, Yale University School of Medicine, New Haven, CT 06511, USA; Department of Genetics, Yale University School of Medicine, New Haven, CT 06510, USA.

Cell Reports
|January 30, 2025
PubMed

Insights

This study reveals that stress granule RNA-binding proteins (RBPs) and their associated mRNAs localize to focal adhesions, enhancing cell migration by regulating focal adhesion size and protein mobility.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Subcellular mRNA localization is critical for biological processes like cell migration.
  • Beta-actin mRNA and ZBP1/IGF2BP1 are known to localize to focal adhesions (FAs) to support cell migration.
  • The presence of other mRNAs and RBPs at FAs remains largely unexplored.

Purpose of the Study:

  • To identify mRNAs and RNA-binding proteins (RBPs) localized at focal adhesions (FAs).
  • To elucidate the mechanism by which these molecules regulate FA function and cell migration.
  • To investigate the role of G3BP1-containing ribonucleoprotein complexes (RNPs) in non-stress conditions.

Main Methods:

  • Identification of hundreds of mRNAs enriched at FAs (FA-mRNAs) using transcriptomic analysis.
  • Characterization of FA-mRNAs' association with stress granule (SG) mRNAs and SG RBPs.
  • Investigation of G3BP1's RNA-dependent binding to FA proteins and the role of its domains in RNP formation and FA localization.

Main Results:

  • Hundreds of FA-mRNAs were identified, sharing characteristics with stress granule (SG) mRNAs.
  • The SG RBP G3BP1 was found to bind FA proteins in an RNA-dependent manner.
  • G3BP1's RNA-binding and dimerization domains are crucial for its FA localization and cell migration.
  • G3BP1 RNPs enhance cell speed by increasing FA protein mobility and FA size.

Conclusions:

  • G3BP1-containing RNPs are recruited to FAs and play a significant role in regulating FA dynamics.
  • This recruitment and subsequent regulation of FA proteins by G3BP1 RNPs are essential for efficient cell migration.
  • The findings highlight a novel role for G3BP1 RNPs in controlling FA function under normal physiological conditions, beyond their known role in stress granules.
Keywords:
CP: Cell biologyCP: Molecular biologyG3BP1RNA localizationcell migrationfocal adhesionsprotein mobilityribonucleoprotein complexes

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