ArticleMolecular and cellular biology2016
Myocardin-Related Transcription Factor A Activation by Competition with WH2 Domain Proteins for Actin Binding.
Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Myocardin-related transcription factor regulates actomyosin contractility and apical junction remodeling during vertebrate neural tube closure.Development (Cambridge, England) · 2025Article
- MRTF: Basic Biology and Role in Kidney Disease.International journal of molecular sciences · 2021Review
- Review
- Mix and (mis-)match - The mechanosensing machinery in the changing environment of the developing, healthy adult and diseased heart.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Myocardin-Related Transcription Factor A (MRTF-A) Regulates the Balance between Adipogenesis and Osteogenesis of Human Adipose Stem Cells.Stem cells international · 2020Article
- IGF2BP1 promotes SRF-dependent transcription in cancer in a m6A- and miRNA-dependent manner.Nucleic acids research · 2019Article
- Regulation of MRTF-A by JMY via a nucleation-independent mechanism.Cell communication and signaling : CCS · 2018Article
- SRF'ing and SAP'ing - the role of MRTF proteins in cell migration.Journal of cell science · 2018Review
- Persistent inhibition of pore-based cell migration by sub-toxic doses of miuraenamide, an actin filament stabilizer.Scientific reports · 2017Article
- Opposite effects of HDAC5 and p300 on MRTF-A-related neuronal apoptosis during ischemia/reperfusion injury in rats.Cell death & disease · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The myocardin-related transcription factors (MRTFs) are coactivators of serum response factor (SRF)-mediated gene expression. Activation of MRTF-A occurs in response to alterations in actin dynamics and critically requires the dissociation of repressive G-actin-MRTF-A complexes. However, the mechanism leading to the release of MRTF-A remains unclear. Here we show that WH2 domains compete directly with MRTF-A for actin binding. Actin nucleation-promoting factors, such as N-WASP and WAVE2, as well as isolated WH2 domains, including those of Spire2 and Cobl, activate MRTF-A independently of changes in actin dynamics. Simultaneous inhibition of Arp2-Arp3 or mutation of the CA region only partially reduces MRTF-A activation by N-WASP and WAVE2. Recombinant WH2 domains and the RPEL domain of MRTF-A bind mutually exclusively to cellular and purified G-actin in vitro The competition by different WH2 domains correlates with MRTF-SRF activation. Following serum stimulation, nonpolymerizable actin dissociates from MRTF-A, and de novo formation of the G-actin-RPEL complex is impaired by a transferable factor. Our work demonstrates that WH2 domains activate MRTF-A and contribute to target gene regulation by a competitive mechanism, independently of their role in actin filament formation.
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