With multiple pathways interacting or converging on SRF, it is considered central to mechanotransduction. NF-kB, zyxin/paxillin, integrin, E-cadherin, Wnt, TGFβ signaling pathways, all represent upstream components of SRF signaling, and as a result, SRF regulates actin-related genes, muscle type-specific genes (i.e., cardiac, smooth, skeletal), as well as genes related to cell survival and apoptosis.
SRF is therefore integral to a vast number of cellular processes, from cell-proliferation, to muscle differentiation and development. It is also important in processes directly related to cytoskeleton dynamics, including cell adhesion and cell migration (reviewed in ).
Importantly, SRF does not directly interact with actin, and is instead activated by one of two classes of cofactors. Specifically, myocardin-related transcription factors (MRTFs), including myocardin itself , and ternary complex factors (TCFs)  . The former is dependent on signaling from the Rho-actin pathway , whereas TCF requires phosphorylation by the MAP kinase pathway. Importantly, these two cofactors compete with each other for mutually exclusive interaction with SRF . SRF localizes to the nucleus in homodimeric form, and once activated by either an MRTF or TCF, will bind with high affinity to the palindromic DNA sequence CC(A/T)2A(A/T)3GG, which is present in the promoter region of each target gene. This sequence is also known as a CArG-box, a C A-rich G –box, or an SRE serum response element .
Despite the large number of SRF target genes, they can generally be grouped into a small number of groups based on their function. Those genes that encode proteins that are involved in the G0-G1 transition of the cell cycle are mostly regulated by the Ras pathway, and in these cases SRF will be activated by a TCF. . However, genes which encode muscle specific proteins involved in contractile functions, cell motility and actin dynamics seem to be regulated by the Rho-MRTF mediated activation of SRF. Actin-related SRF-regulated gene products can be further grouped into structural proteins (e.g., actin, dystrophin, myosin, vinculin), effectors of actin turnover (e.g., cofilin, gelsolin) and regulators of actin dynamics (e.g., talin, filamin) .
Stimulation of Rho-GTPases promotes monomeric G-actin polymerization into F-actin, liberating MRTFs from G-actin and exposing their NLS, which allows their relocation from the cytoplasm to the nucleus. For this reason, if actin polymerization is low, MRTFs are primarily found in the cytoplasm in their inactive, G-actin bound complex (with the exception of myocardin, which seems to be constitutively nuclear ).
Free and activated MRTF gets transported to nucleus due to the presence of the NLS. Like in the cytoplasm, MRTF can bind to free G-actin in the nucleus, and therefore any excess nuclear G-actin can deactivate the MRTF, and promote its export back to the cytoplasm . However, where MRTF remains free in the nucleus, it will associate with SRF through a basic region with adjacent Glu-rich domains . The activated MRTF-SRF complex finally binds to CArG-box to promote the transcription of the target genes.
The described mechanism of MRTF-SRF circuit varies among different tissue and cell types. For example, in smooth, cardiac and skeletal muscle cells and in fibroblasts, the nuclear concentration of MRTFs depends on G-actin concentration, whereas in neurons there is a constantly elevated level of nuclear MRTF . Additionally, there are many positive and negative regulators of the MRTF-SRF circuit. These achieve their effect via competitive binding to either MRTFs or SRF.
Other cofactors can regulate SRF. For example, the GATA, Nkx2-5 and the CRP family induce a positive regulation, whereas LIM-only protein FHL2, histone deacetylase 4, homeodomain protein MSX1 and heart-enriched homeodomain-only cofactor HOP will negatively regulate SRF activity. It is, however, not clear, to what extent these cofactors control SRF by themselves as opposed to acting in conjunction with the MRTFs or TCFs .
With the CArG-box present in the promoters of many muscle development and growth related genes  and with a fundamental role in the regulation of genes related to the actin cytoskeleton , SRF is integral to the cells ability to sense and respond to mechanical cues from its environment.
SRF-signaling has been implicated as a major pathway in the direct regulation of genes responsible for stem cell fate regulation , rigidity sensing , inflammatory migration of immune cells  and morphogenesis .
Conneli et al.  have shown that keratinocytes become spread when grown on stiffer surfaces, and exhibit an increase in the formation of mature focal adhesions with a rapid reorganization of actin filaments. When grown on softer surfaces however, the cells round up, and dense cortical actin network is formed. This ultimately depletes the pool of free cellular G-actin releasing MRTFs, and reduces SRF signaling. The end result is terminal differentiation of the cell
A review by Tyler and Halene suggest a de novo synthesis of actin and other cytoskeletal proteins is mediated by SRF signaling during the trans-epithelial migration of immune cells .
Abnormalities observed in the cytoskeleton of Srf-null embryonic stem cells  suggest that SRF is an important regulator of cytoskeletal dynamics. Park et al. have shown that smooth muscle cells (SMC) specific Srf knock-out is embryonic lethal in mice due to severe defects in gastrointestinal and cardiac developments.