User:Jan.Elias/SynNotch

synNotch receptors are a class of artificially created receptors that are used in syntetic biology applications. They are derived from naturally occuring Notch receptors, which is a family of transmembrane receptors participating in wide range of cellular processes, for example embryogenesis, cardiovascular development, immunity and other.

Structure and function
synNotch receptors have an extremely modular architecture and are comprised of three basic domains, extracellular domain, transmembrane domain and an intracellular domain. Of these three domains, only the transmembrane domain that directs the proteolysis and release of the intracellular domain is retained from the original Notch receptors. Extracellular domain serves as an input sensing platform for various stimuli present on cellular surfaces of cells encountered by the bearer of synNotch receptor and the intracellular domain serves as a transcription factor responsible for functional output of the receptor. Like the Notch receptors, synNotch have their activity triggered by pulling of the transmembrane domain, which activates its proteolytitic activity and transcription factor release in a dose dependent manner. The modality of those receptors can be governed by alterations made to this domain by changing the number of extracellular EGF repeats, which are part of the transmembrane domain. This is demonstrated by high basal activity for some versions of a given receptor, but addition of EGF repeats regulates this activity significantly and the receptor retains its activation potential upon introduction of the correct ligand.