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Open AccessJournal ArticleDOI

Akt Isoforms: A Family Affair in Breast Cancer

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TLDR
In this article, the authors analyzed current literatures on distinct functions of Akt isoforms in breast cancer and proposed an approach to target the Akt signaling pathway for cancer therapy, which is critical to effectively target this pathway.
Abstract
Akt, also known as protein kinase B (PKB), belongs to the AGC family of protein kinases. It acts downstream of the phosphatidylinositol 3-kinase (PI3K) and regulates diverse cellular processes, including cell proliferation, cell survival, metabolism, tumor growth and metastasis. The PI3K/Akt signaling pathway is frequently deregulated in breast cancer and plays an important role in the development and progression of breast cancer. There are three closely related members in the Akt family, namely Akt1(PKBα), Akt2(PKBβ) and Akt3(PKBγ). Although Akt isoforms share similar structures, they exhibit redundant, distinct as well as opposite functions. While the Akt signaling pathway is an important target for cancer therapy, an understanding of the isoform-specific function of Akt is critical to effectively target this pathway. However, our perception regarding how Akt isoforms contribute to the genesis and progression of breast cancer changes as we gain new knowledge. The purpose of this review article is to analyze current literatures on distinct functions of Akt isoforms in breast cancer.

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Beyond Proteolysis-Targeting Chimeric Molecules: Designing Heterobifunctional Molecules Based on Functional Effectors.

TL;DR: Heterobifunctional molecules other than PROTACs are introduced, the limitations of existing molecules are summarized, the main challenges are listed, and perspectives for future research directions are proposed, providing insight into alternative design strategies based on substrate-proximity-based targeting.
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The PI3K/AKT signaling pathway in cancer: Molecular mechanisms and possible therapeutic interventions.

TL;DR: In this paper , a review of the relationship between PI3K/AKT signaling pathway and factors contributing to initiation and development of various cancers is presented, and therapeutic interventions regulating this signaling pathway have been summarized.
Journal ArticleDOI

Role of protein phosphorylation in cell signaling, disease, and the intervention therapy

TL;DR: In this article , the authors analyzed 303 small-molecule protein phosphorylation kinase inhibitors (PKIs) registered and participated in clinical research obtained in a database named Protein Kinase Inhibitor Database (PKIDB), including 68 drugs approved by the Food and Drug Administration of the United States.
Journal ArticleDOI

AKT Serine/Threonine Kinase 2-mediated phosphorylation of Fascin Threonine 403 regulates esophageal cancer progression.

TL;DR: In this article , a novel phosphorylation of Fascin Threonine 403 (Fascin-T403) mediated by AKT serine/threonine kinase 2 (AKT2) was studied using mass spectrometry data from esophageal cancer tissues (iProX database: IPX0002501000).
Journal ArticleDOI

Mir-29b in Breast Cancer: A Promising Target for Therapeutic Approaches

TL;DR: Of particular interest are the data showing that miR-29b1-5p counteracts cell proliferation and migration and reduces stemness in breast tumor cells with a triple negative phenotype, and its possible implication in phenotype-specific management of breast tumors.
References
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Journal ArticleDOI

Akt stimulates aerobic glycolysis in cancer cells

TL;DR: It is suggested that activation of the Akt oncogene is sufficient to stimulate the switch to aerobic glycolysis characteristic of cancer cells and that Akt activity renders cancer cells dependent on aerobic glyCOlysis for continued growth and survival.
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RB and cell cycle progression

TL;DR: It has been shown that Rb protein (pRb) is responsible for a major G1 checkpoint, blocking S-phase entry and cell growth.
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Role of Translocation in the Activation and Function of Protein Kinase B

TL;DR: The results indicate that PI3-K activity is required for translocation of PKB to the plasma membrane, where its activation occurs through phosphorylation of the same sites that are induced by insulin or IGF-1.
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