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Gene Review

Akt2  -  thymoma viral proto-oncogene 2

Mus musculus

Synonyms: 2410016A19Rik, AW554154, PKB, PKB beta, PKBbeta, ...
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Disease relevance of Akt2


High impact information on Akt2

  • The mammary gland defect in female opgl-/- mice is characterized by enhanced apoptosis and failures in proliferation and PKB activation in lobulo-alveolar buds that can be reversed by recombinant OPGL treatment [6].
  • A serine/threonine kinase, named protein kinase B (PKB) for its sequence homology to both protein kinase A and C, has previously been isolated [7].
  • These results suggest a role for PKB in PI(3)K-mediated signal transduction [7].
  • Finally, we show that a constructed Gag-PKB fusion protein, homologous to the v-akt oncogene, displays significantly increased ligand-independent kinase activity [7].
  • These early events lead to activation of the serine-threonine protein kinase Akt, also known as protein kinase B. We show that mice deficient in Akt2 are impaired in the ability of insulin to lower blood glucose because of defects in the action of the hormone on liver and skeletal muscle [8].

Chemical compound and disease context of Akt2


Biological context of Akt2


Anatomical context of Akt2


Associations of Akt2 with chemical compounds

  • The serine/threonine protein kinases Akt1 and Akt2, which have been implicated as mediators of insulin-stimulated glucose uptake, as well as glycogen, lipid, and protein synthesis, were shown to mirror this selectivity in this tissue culture system [15].
  • Akt1 and Akt2 differently regulate muscle creatine kinase and myogenin gene transcription in insulin-induced differentiation of C2C12 myoblasts [16].
  • We measured insulin-stimulated 2-deoxyglucose (2DG) uptake in isolated extensor digitorum longus (EDL) and soleus muscles from male and female wild-type (WT) and Akt2-null (knockout [KO]) mice after ad libitum or calorie-restricted (20 days at 60% of AL) feeding [17].
  • Akt2 encodes a protein-serine/threonine kinase containing a pleckstrin homology domain characteristic of many signaling molecules [18].
  • Interestingly, the phosphorylation level of Akt at Thr308 (Akt2 at Thr309), but not at Ser473 (Akt2 at Ser474), was revealed to correlate well with the accumulation of phosphatidylinositol 3,4,5-trisphosphate modified by overexpression of these PTEN proteins [19].

Regulatory relationships of Akt2

  • Akt2 promoter activity and protein levels were regulated by p38 activation, thus providing a mechanism for communication [20].
  • These results show that activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes to an extent similar to insulin [21].

Other interactions of Akt2


Analytical, diagnostic and therapeutic context of Akt2


  1. Dwarfism, impaired skin development, skeletal muscle atrophy, delayed bone development, and impeded adipogenesis in mice lacking Akt1 and Akt2. Peng, X.D., Xu, P.Z., Chen, M.L., Hahn-Windgassen, A., Skeen, J., Jacobs, J., Sundararajan, D., Chen, W.S., Crawford, S.E., Coleman, K.G., Hay, N. Genes Dev. (2003) [Pubmed]
  2. Defects in secretion, aggregation, and thrombus formation in platelets from mice lacking Akt2. Woulfe, D., Jiang, H., Morgans, A., Monks, R., Birnbaum, M., Brass, L.F. J. Clin. Invest. (2004) [Pubmed]
  3. Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKB beta. Garofalo, R.S., Orena, S.J., Rafidi, K., Torchia, A.J., Stock, J.L., Hildebrandt, A.L., Coskran, T., Black, S.C., Brees, D.J., Wicks, J.R., McNeish, J.D., Coleman, K.G. J. Clin. Invest. (2003) [Pubmed]
  4. Life with a single isoform of akt: mice lacking akt2 and akt3 are viable but display impaired glucose homeostasis and growth deficiencies. Dummler, B., Tschopp, O., Hynx, D., Yang, Z.Z., Dirnhofer, S., Hemmings, B.A. Mol. Cell. Biol. (2006) [Pubmed]
  5. Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CbetaII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40. Patel, N.A., Kaneko, S., Apostolatos, H.S., Bae, S.S., Watson, J.E., Davidowitz, K., Chappell, D.S., Birnbaum, M.J., Cheng, J.Q., Cooper, D.R. J. Biol. Chem. (2005) [Pubmed]
  6. The osteoclast differentiation factor osteoprotegerin-ligand is essential for mammary gland development. Fata, J.E., Kong, Y.Y., Li, J., Sasaki, T., Irie-Sasaki, J., Moorehead, R.A., Elliott, R., Scully, S., Voura, E.B., Lacey, D.L., Boyle, W.J., Khokha, R., Penninger, J.M. Cell (2000) [Pubmed]
  7. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Burgering, B.M., Coffer, P.J. Nature (1995) [Pubmed]
  8. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Cho, H., Mu, J., Kim, J.K., Thorvaldsen, J.L., Chu, Q., Crenshaw, E.B., Kaestner, K.H., Bartolomei, M.S., Shulman, G.I., Birnbaum, M.J. Science (2001) [Pubmed]
  9. Oncoprotein Akt/PKB induces trophic effects in murine models of Parkinson's disease. Ries, V., Henchcliffe, C., Kareva, T., Rzhetskaya, M., Bland, R., During, M.J., Kholodilov, N., Burke, R.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  10. Polyoma middle T antigen activates the Ser/Thr kinase Akt in a PI3-kinase-dependent manner. Summers, S.A., Lipfert, L., Birnbaum, M.J. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  11. Insulin signaling through Akt/protein kinase B analyzed by small interfering RNA-mediated gene silencing. Jiang, Z.Y., Zhou, Q.L., Coleman, K.A., Chouinard, M., Boese, Q., Czech, M.P. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  12. SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes. Sasaoka, T., Wada, T., Fukui, K., Murakami, S., Ishihara, H., Suzuki, R., Tobe, K., Kadowaki, T., Kobayashi, M. J. Biol. Chem. (2004) [Pubmed]
  13. Opposing roles for akt1 and akt2 in rac/pak signaling and cell migration. Zhou, G.L., Tucker, D.F., Bae, S.S., Bhatheja, K., Birnbaum, M.J., Field, J. J. Biol. Chem. (2006) [Pubmed]
  14. Differential contribution of insulin receptor substrates 1 versus 2 to insulin signaling and glucose uptake in l6 myotubes. Huang, C., Thirone, A.C., Huang, X., Klip, A. J. Biol. Chem. (2005) [Pubmed]
  15. Differentiation-dependent suppression of platelet-derived growth factor signaling in cultured adipocytes. Summers, S.A., Whiteman, E.L., Cho, H., Lipfert, L., Birnbaum, M.J. J. Biol. Chem. (1999) [Pubmed]
  16. Akt1 and Akt2 differently regulate muscle creatine kinase and myogenin gene transcription in insulin-induced differentiation of C2C12 myoblasts. Sumitani, S., Goya, K., Testa, J.R., Kouhara, H., Kasayama, S. Endocrinology (2002) [Pubmed]
  17. Akt2 is essential for the full effect of calorie restriction on insulin-stimulated glucose uptake in skeletal muscle. McCurdy, C.E., Cartee, G.D. Diabetes (2005) [Pubmed]
  18. Akt2 mRNA is highly expressed in embryonic brown fat and the AKT2 kinase is activated by insulin. Altomare, D.A., Lyons, G.E., Mitsuuchi, Y., Cheng, J.Q., Testa, J.R. Oncogene (1998) [Pubmed]
  19. Regulation of phosphoinositide metabolism, Akt phosphorylation, and glucose transport by PTEN (phosphatase and tensin homolog deleted on chromosome 10) in 3T3-L1 adipocytes. Ono, H., Katagiri, H., Funaki, M., Anai, M., Inukai, K., Fukushima, Y., Sakoda, H., Ogihara, T., Onishi, Y., Fujishiro, M., Kikuchi, M., Oka, Y., Asano, T. Mol. Endocrinol. (2001) [Pubmed]
  20. Akt2, a novel functional link between p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways in myogenesis. Gonzalez, I., Tripathi, G., Carter, E.J., Cobb, L.J., Salih, D.A., Lovett, F.A., Holding, C., Pell, J.M. Mol. Cell. Biol. (2004) [Pubmed]
  21. Rapid activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes. Ng, Y., Ramm, G., Lopez, J.A., James, D.E. Cell Metab. (2008) [Pubmed]
  22. Akt regulates basal and induced processing of NF-kappaB2 (p100) to p52. Gustin, J.A., Korgaonkar, C.K., Pincheira, R., Li, Q., Donner, D.B. J. Biol. Chem. (2006) [Pubmed]
  23. A new strategy for studying protein kinase B and its three isoforms. Role of protein kinase B in phosphorylating glycogen synthase kinase-3, tuberin, WNK1, and ATP citrate lyase. Sale, E.M., Hodgkinson, C.P., Jones, N.P., Sale, G.J. Biochemistry (2006) [Pubmed]
  24. Chromosome mapping of the mouse Akt2 gene and Akt2 pseudogene. Altomare, D.A., Kozak, C.A., Sonoda, G., Testa, J.R. Cytogenet. Cell Genet. (1996) [Pubmed]
  25. A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes. Hill, M.M., Clark, S.F., Tucker, D.F., Birnbaum, M.J., James, D.E., Macaulay, S.L. Mol. Cell. Biol. (1999) [Pubmed]
  26. Cloning, chromosomal localization and expression analysis of the mouse Akt2 oncogene. Altomare, D.A., Guo, K., Cheng, J.Q., Sonoda, G., Walsh, K., Testa, J.R. Oncogene (1995) [Pubmed]
  27. Expression of mRNA for Akt, serine-threonine protein kinase, in the brain during development and its transient enhancement following axotomy of hypoglossal nerve. Owada, Y., Utsunomiya, A., Yoshimoto, T., Kondo, H. J. Mol. Neurosci. (1997) [Pubmed]
  28. Nerve growth factor promotes activation of the alpha, beta and gamma isoforms of protein kinase B in PC12 pheochromocytoma cells. Andjelković, M., Suidan, H.S., Meier, R., Frech, M., Alessi, D.R., Hemmings, B.A. Eur. J. Biochem. (1998) [Pubmed]
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