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Description

Akt (protein kinase B), a serine/threonine kinase, has emerged as a critical enzyme in signal transduction pathways involved in cell proliferation, apoptosis, angiogenesis, and diabetes. In mammals three isoforms of Akt (alpha, beta, gamma or Akt 1, 2, 3) are reported that exhibit a high degree of homology, but differ slightly in the localization of their regulatory phosphorylation sites. Akt alpha is the predominant isoform in most tissues, whereas the highest expression of Akt beta is observed in the insulin-responsive tissues, and Akt gamma is abundant in brain tissue. Each Akt isoform is composed of three functionally distinct regions: an N-terminal pleckstrin homology (PH) domain that provides a lipid-binding module to direct Akt to PIP2 and PIP3, a central catalytic domain, and a C-terminal hydrophobic motif.