ArticleMolecular biology of the cell2023
BAG6 supports stress fiber formation by preventing the ubiquitin-mediated degradation of RhoA.
Article in Molecular biology of the cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Genome-wide CRISPR screen identifies STK11 as a critical regulator of sialic acid clusters important for influenza A virus attachment.Journal of advanced research · 2026Article
- GLMP promotes EGFR-TKI resistance by activating autophagy and RhoA pathway in non-small cell lung cancer.NPJ precision oncology · 2025Article
- Beyond the Genotype: A Multi-Omic Analysis of APOEe4's Role in Alzheimer's Disease.bioRxiv : the preprint server for biology · 2025Article
- Protein quality control machinery supports primary ciliogenesis by eliminating GDP-bound Rab8-family GTPases.iScience · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rho family of small GTPases is a key regulator of cytoskeletal actin polymerization. Although the ubiquitination of Rho proteins is reported to control their activity, the mechanisms by which the ubiquitination of Rho family proteins is controlled by ubiquitin ligases have yet to be elucidated. In this study, we identified BAG6 as the first factor needed to prevent the ubiquitination of RhoA, a critical Rho family protein in F-actin polymerization. We found that BAG6 is necessary for stress fiber formation by stabilizing endogenous RhoA. BAG6 deficiency enhanced the association between RhoA and Cullin-3-based ubiquitin ligases, thus promoting its polyubiquitination and subsequent degradation, leading to the abrogation of actin polymerization. In contrast, the restoration of RhoA expression through transient overexpression rescued the stress fiber formation defects induced by BAG6 depletion. BAG6 was also necessary for the appropriate assembly of focal adhesions as well as cell migration events. These findings reveal a novel role for BAG6 in maintaining the integrity of actin fiber polymerization and establish BAG6 as a RhoA-stabilizing holdase, which binds to and supports the function of RhoA.
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