| 1991 |
SRF and yeast MCM1 share a conserved 90-amino-acid MADS-box domain that is sufficient for dimerization, DNA binding, and ternary complex formation with accessory proteins (p62TCF for SRF; STE12 and p62TCF for MCM1). Substitution of three specific residues in ARG80 with SRF equivalents (positions 198, 200, 203) conferred p62TCF recruitment, and substitution of four SRF residues with MCM1 equivalents (positions 73, 75, 77, 78) conferred STE12 recruitment, identifying specific amino acids within the shared domain that mediate distinct protein-protein interactions. |
In vitro gel retardation assays, chimeric protein domain swapping, site-directed mutagenesis |
The EMBO journal |
High |
1756729
|
| 1991 |
The N-terminal 98-amino-acid MADS-box domain of MCM1 (ortholog sharing 70% identity with SRF DNA-binding domain) is sufficient for DNA binding, dimerization, viability, and physical interaction with cofactors alpha1, alpha2, and STE12; a ~50 amino acid sub-region within this domain provides contacts with all three cofactors. |
In vitro binding studies with deletion constructs, in vivo reporter assays, yeast complementation |
The EMBO journal |
High |
1756728
|
| 1992 |
SRF and MCM1 have related but distinct DNA-binding specificities: MCM1 selects a consensus (NotC)CCY(A/T)(A/T)(T/A)NN(A/G)G, distinct from the SRF consensus CC(A/T)6GG. Differences in specificity map largely to the N-terminal basic portion of their respective DNA-binding domains. |
In vitro selection of binding sites from random oligonucleotides, carboxylethylation interference analysis, comparative binding affinity assays |
Nucleic acids research |
High |
1630900
|
| 1992 |
MCM1 sets the precise spacing and orientation of alpha2 homeodomain dimers on DNA: alpha2 dimers alone bind inverted, direct, and everted repeat arrangements with equal affinity, but MCM1 restricts binding to only the naturally occurring operator geometry, thereby raising target specificity of the homeodomain protein. |
In vitro DNA binding assays with artificial operators containing half-sites in different arrangements, affinity measurements |
Cell |
High |
1732062
|
| 1992 |
The Elk-1 ETS domain is necessary and sufficient for direct DNA binding, while both the ETS domain and flanking sequences up to amino acid 169 (including a protein-protein interaction region spanning residues 137–169) are required for ternary complex formation with SRF at the c-fos serum response element. A single amino acid substitution in the ETS domain can dramatically alter direct DNA-binding affinity without severely affecting SRF-assisted binding. |
In vitro gel retardation assays with Elk-1 deletion and point-mutant constructs |
Nucleic acids research |
High |
1630903
|
| 1993 |
SAP-1 (isolated by yeast genetic screen) and Elk-1 both function as SRF accessory proteins (p62/TCF class) that form ternary complexes with SRF at the serum response element; only two of the three Elk-1-homologous regions in SAP-1 are required for cooperative interactions with SRF, while the third contains conserved MAP kinase phosphorylation sites. |
Yeast genetic screen for cDNAs with p62/TCF DNA-binding properties, gel retardation ternary complex assays, sequence analysis of conserved phosphorylation sites |
Philosophical transactions of the Royal Society of London. Series B, Biological sciences |
Medium |
8103935
|
| 1998 |
Crystal structure of yeast MATalpha2/MCM1/DNA ternary complex at 2.25 Å reveals that the otherwise flexible N-terminal extension of the alpha2 homeodomain forms a beta-hairpin gripping the MCM1 surface via parallel beta-strand hydrogen bonds and hydrophobic side chains; MCM1-induced DNA bending brings the two proteins closer, facilitating their interaction. A 'chameleon' sequence in alpha2 adopts alpha-helical conformation in one monomer and beta-strand in the other. |
X-ray crystallography at 2.25 Å resolution |
Nature |
High |
9490409
|
| 1997 |
MCM1 uses a DNA-contact mechanism distinct from SRF: 5-bromouracil photo-cross-linking shows MCM1 contacts the major groove at the center of its recognition site (not observed for SRF), and Mcm1-dependent DNA bending requires bases outside the conserved CC(A/T)6GG site that do not affect SRF bending, indicating DNA bending by Mcm1 is sequence-dependent and transcriptionally important even when binding affinity is minimally affected. |
5-bromouracil-mediated photo-cross-linking, gel retardation with extensive base-pair substitution series, in vivo transcriptional reporter assays |
Molecular and cellular biology |
High |
9121436
|
| 1997 |
Mcm1 is phosphorylated in vivo at multiple sites (>8 isoforms by isoelectric focusing), with two major phosphorylation sites in the N-terminal 17 amino acids adjacent to the MADS-box. A unique Mcm1 isoform is induced by osmotic stress (NaCl or KCl), establishing that Mcm1 itself is a target of osmotic stress signal transduction; deletion of the N-terminus or mutation of the primary phosphorylation site impairs growth on high-salt medium. |
Isoelectric focusing of in vivo-labeled protein, deletion and point mutant analysis on high-salt medium, induction experiments with NaCl/KCl |
Molecular and cellular biology |
Medium |
9001236
|
| 1994 |
Specific residues within the MCM1 MADS-box domain (positions 69–81) mediate interaction with alpha1 and STE12 cofactors (a subset also affecting STE12 binding), while interaction with alpha2 requires a distinct mechanism, as nonconservative substitutions at alpha2-contact residues do not significantly affect alpha2-mediated repression. Most lethal mutations affect DNA-binding affinity, and lethality of many such mutations is suppressed by high-copy MCM1. |
In vitro DNA-binding cooperative binding assays, in vivo reporter gene assays, alanine-scanning mutagenesis |
Molecular and cellular biology |
High |
8139556
|
| 1996 |
A hydrophobic patch in the region preceding the alpha2 homeodomain mediates direct protein-protein interaction with Mcm1 (in the absence of DNA), is required for cooperative DNA binding in vitro and transcriptional repression in vivo. A conserved YPWM motif found in homeodomain proteins of insects and mammals can partially substitute for this patch in alpha2, suggesting evolutionary conservation of the interaction mechanism. |
In vitro cooperative DNA-binding assays with alpha2 mutants, in vivo repression assays, comparison with heterologous YPWM-containing peptides |
Molecular and cellular biology |
High |
8628280
|
| 2000 |
In Saccharomyces cerevisiae arginine metabolism, the putative alpha-helix within the MADS-box domain of Mcm1 (and ArgRI) is its primary interaction surface with ArgRIII. Purified GST-ArgRI and ArgRII1-180, or Mcm1 and ArgRII1-180, reconstitute an arginine-dependent DNA-binding activity in mobility shift analysis; ArgRIII stability is required for Mcm1 stability and Mcm1-dependent gene expression. |
Yeast two-hybrid, affinity chromatography with purified proteins, in vitro EMSA reconstitution, in vivo gene expression assays |
Molecular microbiology |
High |
10632874
|
| 2000 |
ArgRII (zinc cluster protein) is the arginine sensor in the ArgR-Mcm1 complex: purified ArgRI and ArgRII1-180 (or Mcm1 and ArgRII1-180) reconstitute arginine-dependent DNA binding in EMSA, and the arginine-binding site maps to the region downstream of ArgRII's zinc cluster domain, sharing identity with bacterial arginine repressor arginine-binding domains. |
In vitro EMSA reconstitution with purified recombinant proteins, arginine-dependence assays, domain deletion analysis |
Molecular and cellular biology |
High |
10688655
|
| 2000 |
SRF-null (Srf−/−) embryonic stem cells show impaired mesodermal differentiation in vitro (failure to activate T/Brachyury), but this impairment is non-cell-autonomous: retinoic acid rescues T activation, SRF re-expression rescues differentiation, and in nude mice Srf−/− ES cells readily form mesodermal derivatives, demonstrating that SRF contributes to mesodermal gene expression in a context-dependent manner. |
Conditional Srf knockout ES cells, in vitro differentiation assays, retinoic acid rescue, teratoma formation in nude mice |
The EMBO journal |
High |
11060034
|
| 2002 |
Mcm1 alanine substitutions in the MADS-box reveal that interaction with alpha2 requires different residues than interaction with alpha1 or Ste12 cofactors: most mutations affecting alpha1/Ste12 binding do not affect alpha2-mediated repression, indicating distinct interaction surfaces within the same domain for different cofactors. |
Systematic alanine-scanning mutagenesis of MADS-box, in vivo transcriptional reporter assays, in vitro DNA-binding assays |
Molecular and cellular biology |
High |
12052870
|
| 2003 |
Mcm7 (MCM helicase subunit) acts as a novel cofactor of Mcm1 in transcriptional regulation: Mcm7 stimulates Mcm1 binding to early cell cycle box (ECB) elements upstream of MCM7, CDC6, and MCM5 promoters; Mcm7 is recruited to these promoters during late M phase while Mcm1 binds constitutively, suggesting Mcm7 modulates periodic expression of early cell cycle genes through Mcm1. |
Gel retardation assays with purified proteins, chromatin immunoprecipitation, in vivo reporter assays, analysis of mcm7 and mcm1 mutants |
The Journal of biological chemistry |
Medium |
12738768
|
| 2002 |
Mcm1 associates globally with chromatin in a punctate pattern, binds cooperatively to multiple sites at autonomously replicating sequences (ARS), and is localized at replication origins in vivo, supporting a direct role for Mcm1 in replication initiation beyond transcriptional regulation of replication genes. |
Chromatin immunoprecipitation, in vivo chromatin association assay, in vitro binding with purified Mcm1, loss-of-function analysis at chromosomal origin |
The Journal of biological chemistry |
Medium |
12473677
|
| 2004 |
SRF directly binds the Bcl-2 promoter in vivo (ChIP) and activates Bcl-2 transcription; reconstitution of Bcl-2 in Srf−/− ES cells rescues apoptosis, demonstrating that SRF-dependent Bcl-2 expression is required for ES cell survival. SRF deficiency also impairs Bcl-xl expression and leads to inappropriate apoptosis in embryoid bodies and pre-gastrulation embryos. |
Chromatin immunoprecipitation, luciferase reporter assays, genetic rescue (Bcl-2 re-expression in Srf−/− ES cells), apoptosis assays |
The EMBO journal |
High |
15057274
|
| 2004 |
FHL2, an SRF target gene, physically interacts with SRF protein and binds promoters of SRF-responsive smooth muscle genes (but not immediate-early gene promoters) in response to RhoA activation. FHL2 antagonizes smooth muscle gene induction by competing with MAL/MRTF-A for SRF binding, creating a negative autoregulatory feedback loop selectively controlling a subset of RhoA-activated SRF targets. |
Large-scale expression profiling, co-immunoprecipitation, chromatin immunoprecipitation, RhoA activation assays, competitive binding assays |
Molecular cell |
High |
15610731
|
| 2004 |
Alpha1 cofactor increases the DNA bend induced by Mcm1 at alpha-specific gene binding sites; this enhanced bending is required for full transcriptional activation. Mcm1 binds alpha-specific gene promoters even in the absence of alpha1 (shown by ChIP), indicating alpha1's function extends beyond Mcm1 recruitment to modulating DNA architecture. |
Chromatin immunoprecipitation, circular permutation DNA-bending assays, in vivo transcriptional reporter assays with bending-defective mutants |
Nucleic acids research |
Medium |
15118075
|
| 2008 |
Disruption of epithelial cell-cell junctions activates SRF-mediated transcription via a Rac1-monomeric actin-MAL/MRTF signaling axis in epithelial cells, distinct from the RhoA-dependent pathway in serum-stimulated fibroblasts. Using clostridial cytotoxins, Rac (but not RhoA) was shown to be required for SRF and target gene induction upon junction dissociation; actomyosin contractility is a prerequisite but not sufficient. |
RNAi knockdown, clostridial cytotoxin-mediated Rho GTPase inhibition, reporter gene assays, dominant-negative and constitutively active GTPase constructs |
Journal of cell science |
Medium |
18334560
|
| 2009 |
RNAi depletion of MRTFs or SRF in breast carcinoma and melanoma cells reduces cell adhesion, spreading, invasion, and motility (without affecting proliferation or inducing apoptosis); MRTF-depleted xenografts show reduced cell motility but normal proliferation. Depletion of MRTFs or SRF prevents lung colonization after intravenous injection. MYH9 (NMHCIIa) and MYL9 (MLC2) are identified as MRTF-dependent SRF target genes also required for invasion and lung colonization. Activated MAL/MRTF-A expression increases lung colonization by poorly metastatic cells. |
RNA interference, xenograft tumor models, intravital imaging, lung colonization assays, gene expression profiling |
Nature cell biology |
High |
19198601
|
| 2008 |
In Alzheimer's disease patients and mouse models, SRF and myocardin are overexpressed in cerebral vascular smooth muscle cells; SRF/MYOCD overexpression transactivates SREBP-2, which downregulates LRP-1 (a key Abeta clearance receptor), generating an Abeta non-clearing VSMC phenotype. Hypoxia stimulates SRF/MYOCD expression in human cerebral VSMCs. |
Immunohistochemistry, overexpression studies in VSMCs, promoter/reporter assays for SREBP-2 transactivation, LRP-1 expression analysis, hypoxia experiments |
Nature cell biology |
Medium |
19098903
|
| 2011 |
Conditional epidermal ablation of Srf in mice leads to reduced cortical actin network in basal cells, failure of mitotic cell rounding, altered phospho-ERM and cortical myosin-IIA distribution, and defects in spindle orientation, asymmetric cell divisions, stratification, and differentiation. Low-dose actin inhibitors in vivo and shRNA knockdown in vitro recapitulate the cortical network loss and rounding defects, linking Srf-driven actin gene expression to cortical actomyosin organization and mitotic shape changes. |
Conditional epidermal Srf knockout mice, low-dose actin inhibitor treatment in vivo, shRNA knockdown in vitro, immunofluorescence of phospho-ERM and myosin-IIA, spindle orientation measurements |
Nature cell biology |
High |
21336301
|
| 2013 |
Inducible endothelial-specific deletion of Srf in postnatal mice abolishes filopodia formation and contractility in tip cells during sprouting angiogenesis, while leaving vascular remodeling intact. VEGF-A induces nuclear accumulation of MRTFs and regulates MRTF/SRF-dependent target genes including Myl9, which is required for endothelial cell migration in vitro. |
Inducible endothelial-specific Srf conditional KO mice, retinal angiogenesis assays, VEGF stimulation, MRTF nuclear localization imaging, in vitro migration assays |
Development (Cambridge, England) |
High |
23674601
|
| 2014 |
GSK-3 directly phosphorylates SRF on a highly conserved serine residue and binds SRF; this serine phosphorylation is required for SRF transcriptional activity and for SRF's interaction with MKL-family cofactors (MKL1 and MKL2) but not with TCF cofactor ELK-1. Axonal growth deficits from GSK-3 inhibition are rescued by constitutively active SRF; the SRF target gene vinculin is sufficient to overcome axonal growth deficits of SRF-deficient and GSK-3-inhibited neurons. |
In vitro kinase assay, co-immunoprecipitation of GSK-3/SRF, site-directed mutagenesis of phosphorylation site, shRNA knockdown, constitutively active SRF rescue, axon outgrowth assays in hippocampal neurons |
The Journal of neuroscience |
High |
24623780
|
| 2015 |
Endothelial-specific depletion of SRF or MRTF-A/-B in mice causes loss of blood-brain barrier integrity and intracerebral hemorrhagic stroke. At the molecular level, SRF/MRTF directly regulate expression of tight junction components (Claudins, ZO proteins), adherens junction components (VE-cadherin, α-Actinin), and basement membrane constituents (Collagen IV), which are downregulated upon SRF depletion. |
Conditional endothelial-specific Srf and Mrtf knockout mice, in vivo MRI for hemorrhage detection, immunofluorescence, gene expression analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
26221020
|
| 2016 |
TCF (ternary complex factor) cofactors act as general antagonists of MRTF-dependent SRF target gene expression by competing directly with MRTFs for access to SRF. TCF inactivation in MEFs inhibits >60% of TPA-inducible gene transcription and impairs cell proliferation; TCF-deficient MEFs exhibit hypercontractile and pro-invasive behavior. SRF ChIP-seq combined with Hi-C identifies over 700 TCF-dependent SRF direct target genes. |
TCF triple inactivation in MEFs, ChIP-seq, Hi-C, RNA-seq, competitive binding assays between TCFs and MRTFs for SRF |
Molecular cell |
High |
27867007
|
| 2017 |
Serum response factor (SRF) binds to the CArG box in the MYH9 promoter and drives its expression; miR-647 directly binds the 3' UTR of SRF mRNA to suppress SRF levels, which in turn reduces MYH9 expression and suppresses gastric cancer metastasis. |
Luciferase 3'UTR reporter assays, ChIP for SRF at MYH9 promoter, overexpression/knockdown experiments, orthotopic GC mouse models |
Theranostics |
Medium |
28900514
|
| 2017 |
Satellite cell-specific Srf deletion abolishes myoblast fusion (required in both fusion partners) without affecting proliferation or differentiation. Srf-null myoblasts lack actin-based finger-like protrusions at fusion sites. Overexpression of an α-actin isoform in Srf-null satellite cells restores actin polymerization and rescues fusion in vitro and in vivo, demonstrating that SRF controls myoblast fusion through maintenance of actin cytoskeleton architecture. |
Satellite cell-specific Srf conditional KO, live imaging of fusion sites, α-actin overexpression rescue, in vivo overload-induced hypertrophy model |
The Journal of cell biology |
High |
29269426
|
| 2018 |
SRF and its coactivator MKL1 bind DNA near hedgehog target genes and form a protein complex with the hedgehog transcription factor GLI1, amplifying GLI1 transcriptional activity. Cytoskeletal activation through Rho and the formin mDia is required for SRF-MKL-driven GLI1 activation. This constitutes a noncanonical hedgehog pathway enabling drug resistance in basal cell carcinomas. |
Multidimensional genomics of human/mouse BCCs, ChIP for SRF/MKL1 near hedgehog target genes, co-immunoprecipitation of SRF-MKL1-GLI1 complex, Rho/mDia inhibition experiments |
Nature medicine |
Medium |
29400712
|
| 2018 |
HDAC6 co-immunoprecipitates with MRTF-A and regulates its acetylation and protein level; HDAC6 inhibition (tubastatin A) or knockdown increases MRTF-A acetylation, total MRTF-A protein, and nuclear SRF transcriptional activity, preserving contractile gene (α-SMA) expression in VSMCs. This is the first demonstration of HDAC6 regulation of the MRTF-A/SRF axis. |
Co-immunoprecipitation, HDAC6 knockdown, pharmacological inhibition (tubastatin A), SRF luciferase reporter, in vivo rat carotid injury model |
JACC. Basic to translational science |
Medium |
30623138
|
| 2019 |
IGF2BP1 promotes SRF expression in cancer cells by binding SRF mRNA and impairing miRNA-directed decay in an m6A-dependent manner, resulting in enhanced SRF-dependent transcriptional activity and upregulation of SRF target genes (including PDLIM7 and FOXK1) that promote tumor cell growth and invasion. |
RNA immunoprecipitation, m6A sequencing, miRNA-reporter assays, RNAi knockdown, gene expression profiling |
Nucleic acids research |
Medium |
30371874
|
| 2020 |
SENP1 deficiency in vascular smooth muscle cells increases SUMOylation of SRF at lysine 143, which reduces SRF lysosomal localization and increases nuclear accumulation, and switches the SRF complex from a contractile phenotype-responsive SRF-myocardin complex to a synthetic phenotype-responsive SRF-ELK1 complex, promoting vascular remodeling and neointimal formation. |
VSMC-specific Senp1 knockout mice, site-directed mutagenesis of SRF K143, co-immunoprecipitation of SRF complexes, subcellular fractionation, ELK inhibitor (AZD6244) treatment, neointima formation assays |
Nature communications |
High |
39134547
|
| 2021 |
Sarcomere disorganization (via Actn2 mutation) increases monomeric cardiac α-actin, which sequesters the SRF cofactor MRTF-A in the cytoplasm and prevents SRF activation. Overexpression of a dominant-negative MRTF-A mutant recapitulates the morphological and transcriptional defects of both Actn2 and Srf mutant cardiomyocytes, placing MRTF-A/SRF downstream of sarcomere integrity in the control of cardiomyocyte maturation. |
Cardiomyocyte-specific Actn2 mutant mice, Srf conditional KO, dominant-negative MRTF-A overexpression, G-actin/F-actin fractionation, MRTF-A nuclear localization imaging, transcriptomic analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
33361330
|
| 2022 |
In LMNA-mutant muscle cells, ERK1/2-phosphorylated cofilin-1 (at T25) binds MRTF-A in the cytoplasm, preventing MRTF-A nuclear entry and SRF stimulation. Reduced MRTF-A/SRF activity decreases expression of ATAT1 (α-tubulin acetyltransferase 1), leading to decreased α-tubulin acetylation and Connexin 43 mislocalization in cardiomyocytes, driving dilated cardiomyopathy. |
Co-immunoprecipitation of phospho-cofilin-1 with MRTF-A, MRTF-A nuclear localization imaging, Atat1 KO mice, tubastatin A treatment of Lmna mutant mice, Cx43 immunofluorescence, cardiac function measurements |
Nature communications |
High |
36550158
|
| 2022 |
Mural cell-specific inducible Srf deletion demonstrates that SRF directs pericyte migration downstream of PDGFRB signaling via MRTF cofactors (PDGFB-dependent SRF activation is MRTF-mediated), and is essential in VSMCs for expression of the contractile machinery; SRF deletion in VSMCs triggers arteriovenous shunt formation. |
Inducible mural cell-specific Srf KO mice, retinal angiogenesis assays, RNA-sequencing, in vivo live imaging, in vitro MRTF-SRF reporter assays with PDGFB stimulation, immunohistology |
Circulation research |
High |
35862101
|
| 2020 |
Exercise induces phosphorylation of a new site on MRTF-B (SRF cofactor), required for its nuclear translocation and subsequent transcription of SRF target gene Fos. High-intensity exercise also phosphorylates histone H3 at serine 10 at SRF target gene loci via MSK1/2; ablation of MSK1/2 prevents this histone phosphorylation, reduces SRF-target gene induction, and prevents increases in protein synthesis after exercise. |
Phosphoproteomics screen in exercised mice, MSK1/2 KO mice, chromatin immunoprecipitation (H3S10p), muscle biopsies from human exercise subjects |
Acta physiologica (Oxford, England) |
Medium |
32408395
|
| 2022 |
The actin cytoskeleton-MRTF-A/SRF signaling cascade transduces extracellular matrix physical cues to modulate circadian clock function. Pharmacological or genetic inhibition of SRF or MRTF-A lengthens circadian period; actin polymerization shortens period. SRF-null or Mrtfa-null cells mimic actin-depolymerizing effects. Per2, Nr1d1, and Nfil3 are identified as direct transcriptional targets of MRTF-A/SRF that mediate the actin dynamics-induced clock response. |
Srf and Mrtfa conditional knockouts, pharmacological inhibition of ROCK/actin polymerization, circadian bioluminescence reporter assays, ChIP identifying Per2/Nr1d1/Nfil3 as direct MRTF-A/SRF targets, integrin/FAK inhibition |
Journal of cell science |
Medium |
36093830
|
| 2010 |
SRF directly binds the frataxin (FXN) promoter (demonstrated by ChIP and EMSA); mutagenesis of the predicted SRF binding site significantly decreases FXN promoter activity; SRF overexpression significantly increases frataxin mRNA and protein levels in HEK293 and SH-SY5Y cells and in Friedreich ataxia patient lymphoblasts. |
Chromatin immunoprecipitation, electrophoretic mobility shift assay, site-directed mutagenesis of SRF binding site, luciferase reporter assays, SRF overexpression in cell lines and patient cells |
PloS one |
Medium |
20808827
|
| 2003 |
B cell receptor activation of SRF occurs via a Src-Syk-Tec-PLCγ-Ca2+ (Lyn-Syk-Btk-PLCγ-Ca2+) pathway. SRF responds to lower Ca2+ concentrations than NFAT and is less dependent on IP3R expression. Calcineurin plays a partial role in SRF activation (in combination with DAG), while calcineurin is fully required for NFAT. Both SRF and NFAT require Rac, Rho, CDC42, and actin; SRF but not NFAT is independent of JNK. |
Pharmacological and dominant-negative inhibition of signaling components, calcium chelation, IP3R-deficient cell lines, reporter assays for SRF and NFAT |
The EMBO journal |
Medium |
12912915
|
| 1999 |
The SRF gene is activated by serum/LPA through a bipartite promoter mechanism requiring both an Sp1-factor binding site (targeted by Ras signaling) and CArG box motifs (targeted by Rho-mediated signals), demonstrating that SRF auto-regulates its own transcription through its CArG binding sites. |
Promoter-reporter assays with mutated SRE/CArG and Sp1 sites, LPA and serum stimulation, dominant-negative Ras and Rho constructs |
Oncogene |
Medium |
10602487
|