AKT2, also known as RAC-beta serine/threonine-protein kinase, is an enzyme that in humans is encoded by the AKT2 gene. It influences metabolite storage as part of the insulin signal transduction pathway.
AKT2, also known as RAC-beta serine/threonine-protein kinase, is an enzyme that in humans is encoded by the AKT2 gene. It influences metabolite storage as part of the insulin signal transduction pathway.
AKT2 is an important signaling molecule in the insulin signaling pathway. It is required to induce glucose transport. In a mouse which is null for AKT1 but normal for AKT2, glucose homeostasis is unperturbed, but the animals are smaller, consistent with a role for AKT1 in growth. In contrast, mice which do not have AKT2, but have normal AKT1, have mild growth deficiency and display a diabetic phenotype (insulin resistance), again consistent with the idea that AKT2 is more specific for the insulin receptor signaling pathway. AKT2 promotes cell migration as well.
This gene is a putative oncogene encoding a protein belonging to the AKT subfamily of serine/threonine kinases that contain SH2-like (Src homology 2-like) domains. The encoded protein is a general protein kinase capable of phosphorylating several known proteins.
AKT2 has important roles in controlling glycogenesis, gluconeogenesis, and glucose transport as part of the insulin signal transduction pathway.
The gene was shown to be amplified and overexpressed in 2 of 8 ovarian carcinoma cell lines and 2 of 15 primary ovarian tumors. Overexpression contributes to the malignant phenotype of a subset of human ductal pancreatic cancers.
Mice lacking Akt2 have a normal body mass, but display a profound diabetic phenotype, indicating that Akt2 plays a key role in signal transduction downstream of the insulin receptor. Mice lacking Akt2 show worse outcome in breast cancer initiated by the large T antigen as well as the neu oncogene.
AKT2 has been shown to interact with:
PDB gallery | |
|---|---|
|
