ArticleThe Journal of cell biology1992
Serum response factor p67SRF is expressed and required during myogenic differentiation of both mouse C2 and rat L6 muscle cell lines.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 92 citations in OpenAlex.
- Srf controls satellite cell fusion through the maintenance of actin architecture.The Journal of cell biology · 2018Article
- The c.-190 C>A transversion in promoter region of protamine1 gene as a genetic risk factor for idiopathic oligozoospermia.Molecular biology reports · 2016Article
- Identification and expression of SRF targeted by miR-133a during early development of Paralichthys olivaceus.Fish physiology and biochemistry · 2015Article
- 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
- miR-411 is up-regulated in FSHD myoblasts and suppresses myogenic factors.Orphanet journal of rare diseases · 2013Article
- Serum response factor is required for cell contact maintenance but dispensable for proliferation in visceral yolk sac endothelium.BMC developmental biology · 2011Article
- KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sites.Molecular and cellular biology · 2010Article
- Comparative in silico analysis identifies bona fide MyoD binding sites within the Myocyte stress 1 gene promoter.BMC molecular biology · 2008Article
- Computational and experimental identification of novel human imprinted genes.Genome research · 2007Article
- Only Akt1 is required for proliferation, while Akt2 promotes cell cycle exit through p21 binding.Molecular and cellular biology · 2006Article
- Genome-wide prediction of imprinted murine genes.Genome research · 2005Article
- Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- SHP-2 positively regulates myogenesis by coupling to the Rho GTPase signaling pathway.Molecular and cellular biology · 2004Article
- Variation in cadherins and catenins expression is linked to both proliferation and transformation of Rhabdomyosarcoma.Oncogene · 2004Article
- Innovative techniques and applications in histochemistry and cell biology.Histochemistry and cell biology · 2003Review
- MyoD distal regulatory region contains an SRF binding CArG element required for MyoD expression in skeletal myoblasts and during muscle regeneration.Molecular biology of the cell · 2003Article
- Targeting of alpha-kinase-anchoring protein (alpha KAP) to sarcoplasmic reticulum and nuclei of skeletal muscle.The Biochemical journal · 2003Article
- Serum response factor plays an important role in the mechanically overloaded plantaris muscle of rats.Histochemistry and cell biology · 2003Article
- Article
- Srf(-/-) ES cells display non-cell-autonomous impairment in mesodermal differentiation.The EMBO journal · 2000Article
Corrections and comments
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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
The 67-kD serum response factor (p67SRF) is a ubiquitous nuclear transcription factor that acts by direct binding to a consensus DNA sequence, the serum response element (SRE), present in the promoter region of numerous genes. Although p67SRF was initially implicated in the activation of mitogen-stimulated genes, the identification of a sequence similar to SRE, the CArG box motif, competent to interact with SRE binding factors in many muscle-specific genes, has led to speculation that, in addition to its function in cell proliferation, p67SRF may play a role in muscle differentiation. Indirect immunofluorescence using affinity-purified antibodies specifically directed against p67SRF reveals that this factor is constitutively expressed and localized in the nucleus of two skeletal muscle cell lines: rat L6 and mouse C2 myogenic cells during myogenic differentiation. This result was further confirmed through immunoblotting and Northern blot analysis. Furthermore, specific inhibition of p67SRF in vivo through microinjection of purified p67SRF antibodies prevented the myoblast-myotube transition and the expression of muscle-specific genes such as the protein troponin T. We further showed that anti-p67SRF injection also inhibited the expression of the myogenic factor myogenin, implying an early requirement for p67SRF in muscle differentiation. These results demonstrate that p67SRF is involved in the process of skeletal muscle differentiation. The potential action of p67SRF via CArG sequences is discussed.
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