How do 14‐3‐3 proteins work? – Gatekeeper phosphorylation and the molecular anvil hypothesis

By Michael B. Yaffe. FEBS Letters, 2002

686 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/1abbc0f2791e326279c911657a85f122d809cbda

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Citations in the corpus

Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, background): “In their turn, these changes can affect enzymatic (biological) activity of a target protein, or mask or reveal specific motifs that regulate its localization, activity, phosphorylation state, and/or stability [60].”
Motif switches: decision-making in cell regulation. (2012, background): “The domain-side of an interaction can induce high-avidity interactions, as illustrated by the dimerisation of 14-3-3 proteins for tight binding to multisite ligands [57].”
The age of crosstalk: phosphorylation, ubiquitination, and beyond. (2007, background): “The same is true for 14-3-3, where two pSer/Thr residues in the same protein or same complex can be bound simultaneously, with one being essential for binding and serving as the gatekeeper and the second being required for specificity and full biological consequences ( Yaffe, 2002 ).”
Characterization of the human heart mitochondrial proteome (2003, background): “Members of the 14-3-3 family are multifunctional proteins that play roles in various cell-signaling events and BAD-mediated apoptosi”
AMPK phosphorylation of raptor mediates a metabolic checkpoint. (2008, background): “of its binding partners via allosteric stabilization of unfavorable states (‘‘the molecular anvil’’ hypothesis) (Yaffe, 2002).”
FoxO transcription factors; Regulation by AKT and 14-3-3 proteins. (2011, background): “Upon target binding, usually as a dimer, 14-3-3 proteins can affect the function of the target protein by several means, including directly modulating the enzymatic activity of the target protein, its protein stability, cellular localization or its association with other proteins [54,59,60].”
The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A (2008, background): “Phosphorylation of synaptopodin and binding to 14-3-3 Similar to the vast majority of 14-3-3–interacting protein”