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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Serum response factor

serum response factor, SRF, MCM1, MCMI
This gene encodes a ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs). [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, Myocardin, V1a, CAN, Rhodopsin
Papers using serum response factor antibodies
MicroRNA-133a protects against myocardial fibrosis and modulates electrical repolarization without affecting hypertrophy in pressure-overloaded adult hearts
Wei Jeanne Y et al., In Journal of Biomedical Science, 2009
... To study the effect of SRF level on cardiac gene expression and function in the mouse heart, we employed the cardiac-specific transgenic approach to increase the ...
Dual roles of myocardin-related transcription factors in epithelial–mesenchymal transition via slug induction and actin remodeling
Sobue Kenji et al., In The Journal of Cell Biology, 1997
... Antitropomyosin (TM311; Sigma-Aldrich), anti–α-SMA (1A4; Sigma-Aldrich), anti–β-actin (AC-15; Sigma-Aldrich), anti-SRF (G-20; Santa Cruz Biotechnology, Inc.), antivinculin (HVIN-1; Sigma-Aldrich), ...
Papers on serum response factor
Nanofibrous clinical-grade collagen scaffolds seeded with human cardiomyocytes induces cardiac remodeling in dilated cardiomyopathy.
Agbulut et al., Paris, France. In Biomaterials, Feb 2016
Acellular collagen scaffolds were first implanted in both healthy mice and those with induced DCM by a cardiac-specific invalidation of serum response factor (SRF).
Resetting the epigenome for heart regeneration.
Hudson et al., Brisbane, Australia. In Semin Cell Dev Biol, Feb 2016
BMP, bone morphogenetic protein; Bvht, Braveheart; CBP, CREB-binding protein; Cdkn, cyclin dependent kinase inhibitor; DOT1L, disruptor of telomeric silencing-1; DNMTs, DNA methyltransferases; eRNAs, enhancer RNAs; ESCs, embryonic stem cells; FGF, fibroblast growth factor; FOX, Forkhead box; Gcn5, general control of amino acid synthesis protein 5; HATs, histone acetyl transferases; HDACs, histone deacteylases; H3K27, histone 3, lysine 27; HMTs, histone methyltransferases; Jmj, Jumonji; JMJD3, Jumonji domain-containing protein 3; KDMs, histone lysine demethylases; lncRNAs, long non-coding RNAs; Mhrt, Myheart; miRNAs, microRNAs; Myh, myosin heavy chain; PRC2, polycomb repressive complex 2; PSCs, pluripotent stem cells; PTM, post-translational modification; SIRTs, Sirtuins; SMYD1, SET and MYND domain containing 1; Srf, serum response factor; TET, Ten-eleven translocation; TGF-β, transforming growth factor beta; TFs, transcription factors; UTX, ubiquitously transcribed tetratricopeptide repeat, X chromosome.
Multi-Phenotypic Role of Serum Response Factor in the Gastrointestinal System.
Ro, Reno, United States. In J Neurogastroenterol Motil, Jan 2016
UNASSIGNED: Serum response factor (SRF) is a master transcription factor of the actin cytoskeleton that binds to highly conserved CArG boxes located within the majority of smooth muscle cell (SMC)-restricted promoters/enhancers.
Myozap Deficiency Promotes Adverse Cardiac Remodeling via Differential Regulation of MAPK/SRF- and β-Catenin/GSK-3β-Signaling.
Frey et al., Kiel, Germany. In J Biol Chem, Jan 2016
Myozap is a recent addition to the list of ID proteins, and has been implicated in SRF signaling.
Stalk-dependent and stalk-independent signaling by the adhesion G protein-coupled receptors GPR56 (ADGRG1) and BAI1 (ADGRB1).
Hall et al., United States. In J Biol Chem, Jan 2016
For G1, however, the results were mixed, with the SL mutant exhibiting robust activity in several signaling assays (including TGFα shedding, activation of NFAT luciferase and beta-arrestin recruitment) but reduced activity relative to ΔNT in a distinct assay (activation of SRF luciferase).
Autoregulatory Control of Smooth Muscle Myosin Light Chain Kinase Promoter by Notch Signaling.
Proweller et al., United States. In J Biol Chem, Jan 2016
In this study, we investigated the combinatorial role of myocardin/serum response factor (SRF) and Notch signaling in the transcriptional regulation of MLCK gene expression.
Transcriptional control of cardiac fibroblast plasticity.
Small et al., Rochester, United States. In J Mol Cell Cardiol, Jan 2016
We will also highlight the major transcriptional regulatory axes that control fibroblast plasticity in the adult heart, including transforming growth factor β (TGFβ)/Smad signaling, the Rho/myocardin-related transcription factor (MRTF)/serum response factor (SRF) axis, and Calcineurin/transient receptor potential channel (TRP)/nuclear factor of activated T-Cell (NFAT) signaling.
Clock-Talk: Interactions between Central and Peripheral Circadian Oscillators in Mammals.
Franken et al., Genève, Switzerland. In Cold Spring Harb Symp Quant Biol, Jan 2016
Signaling through the glucocorticoid receptor and the serum response factor also participate in the phase entrainment of peripheral clocks, and these two pathways are controlled by the SCN independently of feeding-fasting rhythms.
Genomic Instability in Human Pluripotent Stem Cells Arises from Replicative Stress and Chromosome Condensation Defects.
Kerem et al., Jerusalem, Israel. In Cell Stem Cell, Jan 2016
Aneuploid hPSCs show altered levels of actin cytoskeletal genes controlled by the transcription factor SRF, and overexpression of SRF rescues impaired chromosome condensation and segregation defects in aneuploid hPSCs.
Fenofibrate unexpectedly induces cardiac hypertrophy in mice lacking MuRF1.
Willis et al., Chapel Hill, United States. In Cardiovasc Pathol, Nov 2015
Previous work from our group has identified MuRF1's ability to inhibit serum response factor and insulin-like growth factor-1 signaling pathways (via targeted inhibition of cJun as underlying mechanisms).
[MRTFs protein family and its role in pathological stages].
Niewiarowska et al., In Postepy Biochem, 2014
These proteins interact with MADS box transcription factors as well as serum response factors (SRF) thus being engaged into signal transduction, which results from cytoskeleton reorganisation, from cytoplasm to the nucleus.
Redox modification of nuclear actin by MICAL-2 regulates SRF signaling.
Jaffrey et al., New York City, United States. In Cell, 2014
The serum response factor (SRF) binds to coactivators, such as myocardin-related transcription factor-A (MRTF-A), and mediates gene transcription elicited by diverse signaling pathways.
Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling.
Scorrano et al., Genève, Switzerland. In Science, 2013
Gene expression profiling revealed decreased levels of transcription factors transforming growth factor-β/bone morphogenetic protein, serum response factor, GATA4, and myocyte enhancer factor 2, linked to increased Ca(2+)-dependent calcineurin activity and Notch1 signaling that impaired ESC differentiation.
Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics.
Lammerding et al., Ithaca, United States. In Nature, 2013
Laminopathies, caused by mutations in the LMNA gene encoding the nuclear envelope proteins lamins A and C, represent a diverse group of diseases that include Emery-Dreifuss muscular dystrophy (EDMD), dilated cardiomyopathy (DCM), limb-girdle muscular dystrophy, and Hutchison-Gilford progeria syndrome.
Nuclear actin network assembly by formins regulates the SRF coactivator MAL.
Grosse et al., Marburg an der Lahn, Germany. In Science, 2013
In turn, cytoplasmic actin polymerization can promote release of actin from megakaryocytic acute leukemia (MAL) protein for serum response factor (SRF) transcriptional activity.
Serum response factor regulates bone formation via IGF-1 and Runx2 signals.
Chen et al., Birmingham, United States. In J Bone Miner Res, 2012
SRF is important for IGF-1-induced osteoblast differentiation and mineralization via regulating IGF-1 expression and Runx2 transactivity.
A critical cell-intrinsic role for serum response factor in glial specification in the CNS.
Ramanan et al., Saint Louis, United States. In J Neurosci, 2012
SRF plays a critical cell-autonomous role in neural precursor cells to regulate astrocyte and oligodendrocyte specification in vivo and in vitro
Serum response factor and cAMP response element binding protein are both required for cocaine induction of ΔFosB.
Nestler et al., New York City, United States. In J Neurosci, 2012
This study demonistated that Serum response factor and cAMP response element binding protein are both required for cocaine induction of DeltaFosB in Nucleus Accumbens.
Ablation of serum response factor in dopaminergic neurons exacerbates susceptibility towards MPTP-induced oxidative stress.
Parkitna et al., Heidelberg, Germany. In Eur J Neurosci, 2012
Dysfunction or loss of the SRF-activating mitogen-associated kinase pathway under stress conditions in transgenic mice may be part of Parkinson's disease etiology.
Leiomodin 1, a new serum response factor-dependent target gene expressed preferentially in differentiated smooth muscle cells.
Miano et al., Rochester, United States. In J Biol Chem, 2012
Lmod1 is a new SMC-restricted SRF/MYOCD target gene.
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