Rel proto-oncogene proteins are a group of proteins that play a crucial role in regulating cell growth, proliferation, and apoptosis (programmed cell death). They are part of the NF-kappaB (nuclear factor kappa B) family of transcription factors. The name "Rel" comes from the avian reticuloendotheliosis virus strain T, which was first discovered to carry a transforming gene responsible for tumor formation.
The Rel proto-oncogene proteins consist of five main members: RelA (also known as p65), RelB, c-Rel, p50 (a subunit derived from the p105 precursor), and p52 (a subunit derived from the p100 precursor). These proteins are characterized by the presence of a Rel homology domain (RHD) that mediates DNA binding, dimerization, and interaction with inhibitory proteins known as IkappaB.
Upon activation, Rel proteins translocate to the cell nucleus, where they bind to specific DNA sequences called kappaB binding sites, thereby activating the transcription of target genes involved in immune responses, inflammation, cell survival, and proliferation. Dysregulation of Rel proto-oncogene proteins has been implicated in various diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions.
Overall, rel proto-oncogene proteins are critical regulators of cellular homeostasis and their dysfunction can have profound implications for normal cellular processes, contributing to the development and progression of various diseases.
