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14.3.3 proteins are a group of highly conserved proteins that are involved in many vital cellular processes such as metabolism, protein trafficking, signal transduction, apoptosis and cell cycle regulation. 14.3.3 proteins are phospho-serine/-threonine binding proteins.
14.3.3 proteins are a group of highly conserved proteins that are involved in many vital cellular processes such as metabolism, protein trafficking, signal transduction, apoptosis and cell cycle regulation. 14.3.3 proteins are phospho-serine/-threonine binding proteins that have a diverse array of partners including transcription factors, biosynthetic enzymes, cytoskeletal proteins, signaling molecules, apoptosis factors and tumor suppressors.
The 14.3.3 family consists of 7 isoforms; β, γ, ε, σ, ζ, τ and η. 14.3.3 proteins are ubiquitously expressed and self assemble into homo- and heterodimers, with the exception of 14.3.3σ, which exclusively forms homodimers and is found in cells of epithelial origin only. Each monomer contains an independent ligand-binding site, thus the 14.3.3 dimer can interact with two target proteins simultaneously. 14.3.3 proteins are highly rigid structures and ligand binding can induce conformational changes that alter the stability and/or catalytic activity of the ligand. Furthermore, 14.3.3 protein binding can physically occlude sequence-specific or structural motifs on the target that prevent molecular interactions and/or modulate the accessibility of a target protein to modifying enzymes such as kinases, Phosphatases and proteases. In addition, 14.3.3 proteins can act as a scaffold molecule to anchor target proteins within close proximity of one another.
14.3.3 proteins are regulated by post-translational modifications such as phosphorylation, and by the binding of cofactors. Phosphorylation sites on 14.3.3 proteins are not conserved between family members and thus enable selective isoform regulation.
14.3.3 proteins represent an integration point for proliferative, survival, apoptotic and stress signaling pathways. Members of the 14.3.3 protein family enhance the activity of many proteins with proliferative and/or survival functions, such as Raf kinases, and antagonize the activity of proteins that promote cell death and senescence, such as Bad, Bim and Bax. In contrast, 14.3.3σ acts as a tumor suppressor and its expression is upregulated coordinately with p53 and BRAC1. This isoform sequesters cdk1-cyclin B complexes in the cytoplasm, and thus delays cell cycle progression. 14.3.3σ is also a crucial regulator of translation during mitosis.
Because many 14.3.3 interactions are phosphorylation dependent, 14.3.3 proteins have been integrated into the core regulatory pathways that are crucial for normal growth and development. 14.3.3 proteins are directly involved in cellular processes such as cytokinesis, cell-contact inhibition, anchorage-independent growth and cell adhesion, and it is these pathways that often become dysregulated in disease states such as cancer. Recent research has also demonstrated an involvement of 14.3.3 proteins as "reader" domains of epigenetic marks.
Tocris offers the following scientific literature for 14.3.3 Proteins to showcase our products. We invite you to request* or download your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
In normal cells, each stage of the cell cycle is tightly regulated, however in cancer cells many genes and proteins that are involved in the regulation of the cell cycle are mutated or over expressed. Adapted from the 2015 Cancer Product Guide, Edition 3, this poster summarizes the stages of the cell cycle and DNA repair. It also highlights strategies for enhancing replicative stress in cancer cells to force mitotic catastrophe and cell death.
There are two currently recognized forms of programmed cell death: apoptosis and necroptosis. This poster summarizes the signaling pathways involved in apoptosis, necroptosis and cell survival following death receptor activation, and highlights the influence of the molecular switch, cFLIP, on cell fate.
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