serum response factor
serum response factor
Resetting the epigenome for heart regeneration.
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.
Transcriptional control of cardiac fibroblast plasticity.
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.
[MRTFs protein family and its role in pathological stages].
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.
Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics.
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.