The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development

By D. Morrison. Trends in Cell Biology, 2008

622 citations recorded by the source corpus.

The highly conserved 14-3-3 protein family has risen to a position of importance in cell biology owing to its involvement in vital cellular processes, such as metabolism, protein trafficking, signal transduction, apoptosis and cell-cycle regulation. The 14-3-3 proteins are phospho-serine/phospho-threonine binding proteins that interact with a diverse array of binding partners. Because many 14-3-3 interactions are phosphorylation-dependent, 14-3-3 has been tightly integrated into the core phospho-regulatory pathways that are crucial for normal growth and development and that often become dysregulated in human disease states such as cancer. This review examines the recent advances that further elucidate the role of 14-3-3 proteins as integrators of diverse signaling cues that influence cell fate decisions and tumorigenesis.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/fac6d48cb42df61292b2a4428c6b433bb3ffc403

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In Cell Biology

1. L. Galluzzi
2. Guido Kroemer
3. Xaralabos Varelas

In Molecular Biology

1. L. Galluzzi
2. Guido Kroemer
3. Simone Fulda
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5. Douglas R. Green
6. Beth Levine
7. Oliver Kepp
8. Thomas G. Cotter

Citations in the corpus

• FoxO transcription factors; Regulation by AKT and 14-3-3 proteins. (2011, background): “14-3-3 proteins are a family of evolutionary conserved modulator proteins that regulate multiple signaling pathways in the cell through binding to specific Ser/Thr-phosphorylated motifs on target proteins (reviewed in [52–54]).”
• Targeting mitochondria for cancer therapy (2010, background): “The 14-3-3 protein family includes cytosolic multifunctional phosphoserine binding proteins that can interact with (and inhibit) multiple clients, including the pro-apoptotic factors BAX and BA”
• The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease (2014, background): “Of note, TAZ/YAP cytoplasmic recruitment relies on binding to 14-3-3 proteins, which themselves have extended connections with a wide range of polarity regulators (Morrison, 2009).”