Proximity Ligation Analysis of protein-protein interactions between CAMK2A and SMAD2. HeLa cells were stained with anti-CAMK2A rabbit purified polyclonal 1:1200 and anti-SMAD2 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq
MAD, mothers against decapentaplegic homolog 2,Mad protein homolog,Mad, mothers against decapentaplegic homolog 2,Mad-related protein 2,SMAD, mothers against DPP homolog 2,Sma- and Mad-related protein 2,mother against DPP homolog 2