#G3BP1
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration: Cell Reports

www.cell.com/cell-reports...

Amazing work by Liana Boraas, Mengwei Hu, ..., @christinemayr.bsky.social, Siyuan Wang, @nicolilab.bsky.social.
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration
Boraas et al. identify that mRNAs and the stress granule RNA-binding protein G3BP1 form ribonucleoprotein (RNP) complexes at FAs. These RNPs regulate FA protein mobility and cell migration under norma...
www.cell.com
January 31, 2025 at 2:52 PM
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration: Cell Reports www.cell.com/cell-reports...
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration
Boraas et al. identify that mRNAs and the stress granule RNA-binding protein G3BP1 form ribonucleoprotein (RNP) complexes at FAs. These RNPs regulate FA protein mobility and cell migration under norma...
www.cell.com
October 12, 2025 at 6:55 PM
According to new research, the G3BP1 protein helps cancer cells evade chemotherapy. Targeting this protein could enhance treatment efficacy!👇
#G3BP1 #cancer #bone
@brjournal.bsky.social
www.nature.com/articles/s41...
August 29, 2025 at 5:48 AM
Scientists Discover How SARS-CoV-2 Hijacks G3BP1 Triggering Dangerous Fat Metabolism Changes

www.thailandmedical.news/news/scienti...
Scientists Discover How SARS-CoV-2 Hijacks G3BP1 Triggering Dangerous Fat Metabolism Changes - Thailand Medical News
www.thailandmedical.news
October 31, 2025 at 3:42 AM
Our CNS regeneration work has now been published in @PNAS. It was a huge undertaking in collaboration with @Twiss @Benowitz @WardLab_Emory @KristyWelshhans @Marktuszynski @jenniferDulin
@ArthurEnglish @JohnHolule labs. Thank you all, and @MerkinPnnrCtr, for funding.

www.pnas.org/doi/10.1073/...
Disruption of G3BP1 granules promotes mammalian CNS and PNS axon regeneration | PNAS
Depletion or inhibition of core stress granule proteins, G3BP1 in mammals and TIAR-2 in Caenorhabditis elegans, increases the growth of spontaneous...
www.pnas.org
February 28, 2025 at 2:16 PM
Competing Molecular Interactions Govern the Dynamical Arrest of G3BP1 Condensates https://www.biorxiv.org/content/10.64898/2026.07.31.741769v1
August 1, 2026 at 4:49 AM
Aldolase-regulated G3BP1/2+ condensates control insulin mRNA storage in beta cells
Esteban Quezada, Michele Solimena et al.
www.embopress.org/doi/full/10....
May 12, 2025 at 12:04 PM
Protein Disulfide Isomerase (PDI) disassembles TDP-43/G3BP1 condensates and antagonizes TDP-43 aggregates.

By Jia-Qi Liu, ..., Mengchao Cui, Yi Liang, et al.

advanced.onlinelibrary.wiley.com/doi/10.1002/...
May 25, 2026 at 2:47 PM
Study from India shows SARS-CoV-2 hijacks host stress protein G3BP1 for replication.

Drugs fluspirilene & WIN-62577 disrupt this interaction, blocking viral replication with EC50 ~1.8 μM.

Promising for antivirals.

pubs.acs.org/doi/10.1021/...
Disruption of Molecular Interactions between the G3BP1 Stress Granule Host Protein and the Nucleocapsid (NTD-N) Protein Impedes SARS-CoV-2 Virus Replication
The Ras GTPase-activating protein SH3-domain-binding protein 1 (G3BP1) serves as a formidable barrier to viral replication by generating stress granules (SGs) in response to viral infections. Interest...
pubs.acs.org
December 22, 2024 at 1:28 PM
G3BP1 (GTPase-activating protein-binding protein 1) is a multifunctional RNA-binding protein that researchers now report also acts as a molecular scaffold that facilitates Golgi & lysosomal homeostasis maintenance
www.nature.com/articles/s41...
August 28, 2026 at 11:16 PM
“RNA condensers” for SGs and your thoughts…
Nice work from the Parker lab!
#RNA #RNAsky
G3BP1 promotes intermolecular RNA-RNA interactions during RNA condensation: Molecular Cell www.cell.com/molecular-ce...
G3BP1 promotes intermolecular RNA-RNA interactions during RNA condensation
Parker et al. demonstrate that some proteins responsible for organizing ribonucleoprotein granules can chaperone intermolecular RNA-RNA interactions in addition to their role in scaffolding. These findings cement RNA-RNA interaction networks as a key component of granules, highlighting the need to further explore the regulation of RNA dynamics within granules.
www.cell.com
December 6, 2024 at 2:19 PM
A lovely paper out of the Locker lab from Dr. Marques! Picornaviruses really hate G3BP1.

Methodical breakdown of the antiviral role of RNA granules vs granule proteins, not an easy thing to do.

Worth reading for the stunning microscopy alone!

Congrats
July 14, 2026 at 5:49 PM
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration www.sciencedirect.com/science/arti...
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration
The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration. For instance, β-actin mRNA and its assoc…
www.sciencedirect.com
February 24, 2025 at 10:13 AM
It's celebration time: our first contribution to a better understanding of RNA structure and dynamics in biomolecular condensates together with Alberti lab - cool data from in vitro to in condenso to in vivo take a look 👇 @cmcb-tud.bsky.social @tudresden.bsky.social
www.cell.com/molecular-ce...
G3BP-driven RNP granules promote inhibitory RNA-RNA interactions resolved by DDX3X to regulate mRNA translatability
Trussina et al. demonstrate that the storage of mRNA molecules inside G3BP1-driven RNP granules facilitates the formation of RNA-RNA interactions, preventing the mRNA from being translated. The DEAD-box helicase DDX3X facilitates RNP granule dissolution by attenuating these inhibitory RNA-RNA interactions to aid restart of mRNA translation.
www.cell.com
December 26, 2024 at 4:05 PM
“G3BP1 depletion, observed in Parkinson’s Disease, drives Golgi–lysosome–autophagy defects”

This work expands the functional landscape of G3BP1 beyond stress granule assembly, revealing a role in Golgi and lysosomal homeostasis through beta-COP regulation
nature.com/articles/s41...
G3BP1 depletion, observed in Parkinson’s Disease, drives Golgi–lysosome–autophagy defects - Cell Death & Differentiation
Cell Death & Differentiation - G3BP1 depletion, observed in Parkinson’s Disease, drives Golgi–lysosome–autophagy defects
nature.com
August 27, 2026 at 12:19 PM
Stress granules (SGs) form in response to viral infection & serve as a hub for the cell’s innate immune responses. It’s known that N prevents SG formation, an ability traced to its ITGF motif at N:15-18, which binds the key SG protein G3BP1.
21/34
threadreaderapp.com/thread/17789...
May 26, 2025 at 4:11 PM
Heat stress-induced condensation of G3BP1 in perinuclear P-bodies in C. elegans' germline https://www.biorxiv.org/content/10.64898/2026.03.05.709961v1
March 9, 2026 at 4:34 AM
Alphaviral capsid proteins inhibit stress granule assembly via competitive RNA binding with G3BP1 https://www.biorxiv.org/content/10.64898/2025.12.01.691496v1
December 2, 2025 at 11:30 PM