AKT2: A Promising Drug Target and Biomarker for Prostate and Lung Cancer

Target Name: AKT2

NCBI ID: G208

AKT2: A Promising Drug Target and Biomarker for Prostate and Lung Cancer

Prostate and lung cancer are two of the leading causes of cancer-related deaths worldwide. The development of new treatments and biomarkers for these diseases remains a major focus of research. One of the promising targets for cancer research is the protein kinase Akt-2 (AKT2), which has been identified as a potential drug target and biomarker for prostate and lung cancer. In this article, we will explore the biology of AKT2, its role in cancer progression, and its potential as a drug target and biomarker.

The Biology of AKT2

AKT2 is a protein that is expressed in a variety of tissues, including the brain, pancreas, and testes. It is a key regulator of cell growth and metabolism, and its levels have been linked to cancer progression. Several studies have identified AKT2 as a potential drug target for prostate and lung cancer.

In prostate cancer, AKT2 has been shown to promote the growth and survival of cancer cells. Several studies have also shown that inhibiting AKT2 signaling can be an effective way to treat prostate cancer. One of the main mechanisms by which AKT2 promotes cancer cell growth is through the inhibition of the androgen receptor (AR), which is responsible for regulating male sexual function. In prostate cancer, the deregulation of AR leads to the growth and survival of cancer cells.

In lung cancer, AKT2 has been shown to promote the formation of new blood vessels, which is a key factor in the development of new tumors. The formation of new blood vessels allows cancer cells to receive the necessary oxygen and nutrients for growth, leading to the formation of new tumors.

In addition to its role in cancer growth, AKT2 has also been shown to play a key role in the regulation of cell death. It is a transcription factor that is involved in the regulation of cell apoptosis, which is the process by which cells die when they have reached their maximum number of copies. The deregulation of AKT2 has been linked to the development of cancer, as it allows cancer cells to evade the cell death mechanisms that are normally in place.

Potential as a Drug Target

The potential of AKT2 as a drug target is due to its unique biology and the fact that it is involved in the regulation of multiple cellular processes. Several studies have shown that inhibiting the AKT2 signaling pathway can be an effective way to treat prostate and lung cancer.

One of the main advantages of AKT2 as a drug target is its druggability. The AKT2 kinase is a good candidate for inhibition due to its unique structure and the fact that it has multiple interacting residues. Several small molecules have been shown to be potent inhibitors of AKT2, including a range of compounds that are currently in clinical trials.

In addition to its potential as a drug target, AKT2 has also been shown to be a potential biomarker for prostate and lung cancer. The deregulation of AKT2 has been linked to the development of both cancer types. For example, studies have shown that individuals with advanced prostate cancer are characterized by increased levels of AKT2.

Biomarker Potential

AKT2 has also been shown to be a potential biomarker for prostate and lung cancer. The deregulation of AKT2 has been linked to the development of both cancer types. For example, studies have shown that individuals with advanced prostate cancer are characterized by increased levels of AKT2.

In addition to its potential as a biomarker, AKT2 has also been shown to be involved in the regulation of multiple cellular processes. It is a transcription factor that is involved in the regulation of cell apoptosis, which is the process by which cells die when they have reached their maximum number of copies. The deregulation of AKT2 has been linked to

Protein Name: AKT Serine/threonine Kinase 2

Functions: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development

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