ArticleProceedings of the National Academy of Sciences of the United States of America2006
Serum response factor MADS box serine-162 phosphorylation switches proliferation and myogenic gene programs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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Who cites it
37 citing papers in PubMed, 71 citations in OpenAlex.
- Adapting cytoskeleton-mitochondria patterning with myocyte differentiation by promyogenic PRR33.Cell death and differentiation · 2025Article
- Recent advances in serum response factor posttranslational modifications and their therapeutic potential in cardiovascular and neurological diseases.Vascular pharmacology · 2024Review
- STEMIN and YAP5SA, the future of heart repair?Experimental biology and medicine (Maywood, N.J.) · 2024Review
- Lysine methylation signaling in skeletal muscle biology: from myogenesis to clinical insights.The Biochemical journal · 2023Review
- Floral Homeotic Factors: A Question of Specificity.Plants (Basel, Switzerland) · 2023Review
- Glioma pathogenesis-related protein 1 performs dual functions in tumor cells.Cancer gene therapy · 2022Review
- Serum response factor-cofactor interactions and their implications in disease.The FEBS journal · 2021Review
- A GSK3-SRF Axis Mediates Angiotensin II Induced Endothelin Transcription in Vascular Endothelial Cells.Frontiers in cell and developmental biology · 2021Article
- Conservation and diversity of the regulators of cellulolytic enzyme genes in Ascomycete fungi.Current genetics · 2017Review
- Redox regulation of the actin cytoskeleton and its role in the vascular system.Free radical biology & medicine · 2017Review
- Olfactomedin 2 Regulates Smooth Muscle Phenotypic Modulation and Vascular Remodeling Through Mediating Runt-Related Transcription Factor 2 Binding to Serum Response Factor.Arteriosclerosis, thrombosis, and vascular biology · 2017Article
- Nuclear PTEN functions as an essential regulator of SRF-dependent transcription to control smooth muscle differentiation.Nature communications · 2016Article
- Article
- SRF regulates craniofacial development through selective recruitment of MRTF cofactors by PDGF signaling.Developmental cell · 2014Article
- SRF phosphorylation by glycogen synthase kinase-3 promotes axon growth in hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- G-protein coupled receptor 56 promotes myoblast fusion through serum response factor- and nuclear factor of activated T-cell-mediated signalling but is not essential for muscle development in vivo.The FEBS journal · 2013Article
- Analysis of the Sonic Hedgehog signaling pathway in normal and abnormal bladder development.PloS one · 2013Article
- Adhesion regulates MAP kinase/ternary complex factor exchange to control a proliferative transcriptional switch.Current biology : CB · 2012Article
- Mechanism of fibrotic cardiomyopathy in mice expressing truncated Rho-associated coiled-coil protein kinase 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Signaling mechanisms that regulate smooth muscle cell differentiation.Arteriosclerosis, thrombosis, and vascular biology · 2011Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
Phosphorylation of a cluster of amino acids in the serum response factor (SRF) "MADS box" alphaI coil DNA binding domain regulated the transcription of genes associated with proliferation or terminal muscle differentiation. Mimicking phosphorylation of serine-162, a target of protein kinase C-alpha, with an aspartic acid substitution (SRF-S162D) completely inhibited SRF-DNA binding and blocked alpha-actin gene transcription even in the presence of potent myogenic cofactors, while preserving c-fos promoter activity because of stabilization of the ternary complex via Elk-1. Introduction of SRF-S162D into SRF null ES cells permitted transcription of the c-fos gene but was unable to rescue expression of myogenic contractile genes. Transition of proliferating C2C12 myoblasts to postfusion myocytes after serum withdrawal was associated with a progressive decline in SRF-S162 phosphorylation and an increase in alpha-actin gene expression. Hence, the phosphorylation status of serine-162 in the alphaI coil may constitute a novel switch that directs target gene expression into proliferation or differentiation programs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.