ArticleThe Biochemical journal2002
Increased actin polymerization reduces the inhibition of serum response factor activity by Yin Yang 1.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- Single cell RNA analysis uncovers the cell differentiation and functionalization for air breathing of frog lung.Communications biology · 2024Article
- Deletion of Smooth Muscle O-GlcNAc Transferase Prevents Development of Atherosclerosis in Western Diet-Fed Hyperglycemic ApoEInternational journal of molecular sciences · 2023Article
- Rho/SRF Inhibitor Modulates Mitochondrial Functions.International journal of molecular sciences · 2022Article
- YY1 directly interacts with myocardin to repress the triad myocardin/SRF/CArG box-mediated smooth muscle gene transcription during smooth muscle phenotypic modulation.Scientific reports · 2020Article
- Lamin A/C deficiency enables increased myosin-II bipolar filament ensembles that promote divergent actomyosin network anomalies through self-organization.Molecular biology of the cell · 2020Article
- A C2H2 zinc finger protein FEMU2 is required for fox1 expression in Chlamydomonas reinhardtii.PloS one · 2014Article
- Epigenetic regulation of muscle phenotype and adaptation: a potential role in COPD muscle dysfunction.Journal of applied physiology (Bethesda, Md. : 1985) · 2013Review
- The actin-MRTF-SRF gene regulatory axis and myofibroblast differentiation.Journal of cardiovascular translational research · 2012Review
- Yin yang 1 is a novel regulator of pulmonary fibrosis.American journal of respiratory and critical care medicine · 2011Article
- Differential display of DNA-binding proteins reveals heat-shock factor 1 as a circadian transcription factor.Genes & development · 2008Article
- Cytoplasmic YY1 is associated with increased smooth muscle-specific gene expression: implications for neonatal pulmonary hypertension.The American journal of pathology · 2005Article
- Binding of serum response factor to cystic fibrosis transmembrane conductance regulator CArG-like elements, as a new potential CFTR transcriptional regulation pathway.Nucleic acids research · 2005Article
- Selective modulation of the SM22alpha promoter by the binding of BTEB3 (basal transcription element-binding protein 3) to TGGG repeats.The Biochemical journal · 2003Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent evidence has implicated CC(A/T(richG))GG (CArG) boxes, binding sites for serum response factor (SRF), in the regulation of expression of a number of genes in response to changes in the actin cytoskeleton. In many cases, the activity of SRF at CArG boxes is modulated by transcription factors binding to overlapping (e.g. Yin Yang 1, YY1) or adjacent (e.g. ets) binding sites. However, the mechanisms by which SRF activity is regulated by the cytoskeleton have not been determined. To investigate these mechanisms, we screened for cells that did or did not increase the activity of a fragment of the promoter for a smooth-muscle (SM)-specific gene SM22alpha, in response to changes in actin cytoskeletal polymerization induced by LIM kinase. These experiments showed that vascular SM cells (VSMCs) and C2C12 cells increased the activity of promoters containing at least one of the SM22alpha CArG boxes (CArG near) in response to LIM kinase, whereas P19 cells did not. Bandshift assays using a probe to CArG near showed that P19 cells lacked detectable YY1 DNA binding to the CArG box in contrast with the other two cell types. Expression of YY1 in P19 cells inhibited SM22alpha promoter activity and conferred responsiveness to LIM kinase. Mutation of the CArG box to inhibit YY1 or SRF binding indicated that both factors were required for the LIM kinase response in VSMCs and C2C12 cells. The data indicate that changes in the actin cytoskeletal organization modify SRF activity at CArG boxes by modulating YY1-dependent inhibition.
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