Transcriptional enhanced associate domain (TEAD) proteins are a transcription factor mostly present in chromatin components . TEAD transcription factors play an indispensable role in cell proliferation, tissue growth homeostasis, stem cell self-renewal and tumorigenesis. In the biological signal transduction network, TEADs coordinate a variety of signal transduction pathways. Among them, the researches on the Hippo, Wnt, transforming growth factor beta (TGFβ), and epidermal growth factor receptor (EGFR) pathways are more popular, especially the Hippo-YAP/TAZ pathway. TEADs are folded globular proteins that contain multiple different binding pockets. The N-terminal has a DNA binding domain (DBD), which is about 80–90 amino acids in length; the C-terminal has a YAP/TAZ/VgLL binding domain (YBD), which is about 220 amino acids in length. Besides DBD and YBD, it has been found that TEADs have a deep hydrophobic palmitate binding pocket (PBP) by Christian N. Cunningham's team in 2016. The conserved cysteine residues in the pockets are connected with palmitate to make TEADs S-palmitylation, and this process is occurring automatically. TEADs palmitoylation plays a role in checking protein levels in cells, which is very important for the correct folding and stability of TEADs. This lipid-binding pocket can be also occupied by other lipids such as myristate. Here you can see how myristate can bound human TEAD2 transcription factor, as obtained from the corresponding crystal structure (PDB code: 8P29)

#molecularart ... #transcription ... #lipid ... #pocket ... #myristate ... #xray

Structure rendered with @proteinimaging and depicted with @corelphotopaint