Biology:AKT2

From HandWiki

AKT2, also known as RAC-beta serine/threonine-protein kinase,[1] is an enzyme that in humans is encoded by the AKT2 gene.[2] It influences metabolite storage as part of the insulin signal transduction pathway.[1]

Function

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.[3] AKT2 promotes cell migration as well.[4]

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.[5]

AKT2 has important roles in controlling glycogenesis, gluconeogenesis, and glucose transport as part of the insulin signal transduction pathway.[1]

Clinical significance

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.[5]

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.[6]

Interactions

AKT2 has been shown to interact with:

References

  1. ↑ 1.0 1.1 1.2 "Chapter 37 - Lipodystrophy Syndromes" (in en). Endocrinology: Adult and Pediatric (Seventh ed.). Philadelphia: W.B. Saunders. January 2016. pp. 648–661.e5. doi:10.1016/b978-0-323-18907-1.00037-8. ISBN 978-0-323-18907-1. http://www.sciencedirect.com/science/article/pii/B9780323189071000378. Retrieved 2020-12-18. 
  2. ↑ "AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas". Proceedings of the National Academy of Sciences of the United States of America 89 (19): 9267–9271. November 1992. doi:10.1073/pnas.89.19.9267. PMID 1409633. Bibcode: 1992PNAS...89.9267C. 
  3. ↑ "Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKB beta". The Journal of Clinical Investigation 112 (2): 197–208. July 2003. doi:10.1172/JCI16885. PMID 12843127. 
  4. ↑ Cite error: Invalid <ref> tag; no text was provided for refs named Pal_2023
  5. ↑ 5.0 5.1 "Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=208. 
  6. ↑ "Akt1 and Akt2: differentiating the aktion". Histology and Histopathology 26 (5): 651–662. 2011. doi:10.14670/HH-26.651. PMID 21432781. 
  7. ↑ "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2". Oncogene 18 (35): 4891–4898. September 1999. doi:10.1038/sj.onc.1203080. PMID 10490823. 
  8. ↑ "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex". Journal of Biological Chemistry 278 (48): 47922–47927. November 2003. doi:10.1074/jbc.M307357200. PMID 14504284. 
  9. ↑ "Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family". Journal of Biological Chemistry 277 (5): 3743–3751. February 2002. doi:10.1074/jbc.M107069200. PMID 11707444. 
  10. ↑ "The protooncogene TCL1 is an Akt kinase coactivator". Molecular Cell 6 (2): 395–407. August 2000. doi:10.1016/S1097-2765(00)00039-3. PMID 10983986. 

Further reading



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