DDIT4 Human

DDIT4 is known to regulate the activity of the mammalian target of rapamycin complex 1 (mTORC1), a key player in cell growth and metabolism. The inhibition of mTORC1 by DDIT4 is mediated through a pathway involving AKT1, the TSC1-TSC2 complex, and the GTPase RHEB. This regulation is essential for maintaining cellular energy levels and responding to cellular stress, such as hypoxia and DNA damage .

In response to DNA damage, DDIT4 regulates p53-mediated apoptosis by affecting mTORC1 activity. This protein is also involved in the defense against viral protein synthesis and virus replication, highlighting its role in the immune response .

DDIT4 is predominantly located in the cytosol and is expressed in various tissues. Its expression is induced by stress conditions, including hypoxia and DNA damage. The protein’s role in hypoxia response varies depending on the cell type; for instance, it mediates mTORC1 inhibition in fibroblasts and thymocytes but not in hepatocytes .

Mutations or dysregulation of DDIT4 have been associated with several diseases, including squamous cell carcinoma and paranoid schizophrenia. The gene’s involvement in critical cellular pathways makes it a potential target for therapeutic interventions in cancer and other diseases related to cellular stress responses .

Recombinant human DDIT4 is a form of the protein produced through recombinant DNA technology, which involves inserting the DDIT4 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its function, interactions, and potential therapeutic uses.