14.3.3 Proteins

Supporting information

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.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
14-3-3β Human YWHAB NM_003404 P31946
Mouse Ywhab NM_018753 Q9CQV8
Rat Ywhab NM_019377 P35213
14-3-3ε Human YWHAE NM_006761 P62258
Mouse Ywhae NM_009536 P62259
Rat Ywhae NM_031603 P62260
View all 14-3-3 Protein Gene Data »

Literature for 14.3.3 Proteins

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Cancer Research Product Guide

Cancer Research Product Guide

Our Cancer Research Guide highlights over 750 products for cancer research. Request copy or view PDF today.

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Programmed Cell Death

Written by Bram van Raam and Guy Salvesen

Programmed Cell Death Life Science Poster

Our Programmed Cell Death poster gives a summary of the signaling pathways involved in apoptosis, necroptosis and cell survival. Request copy or view PDF today.

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Apoptosis Pathway

Apoptosis Signaling Pathway

Apoptosis is a mechanism of cell death which occurs after sufficient cellular damage. View pathway or download PDF today.

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