Characterization of the interaction of Raf‐1 with ras p21 or 14‐3‐3 protein in intact cells

@article{Koyama1995CharacterizationOT,
  title={Characterization of the interaction of Raf‐1 with ras p21 or 14‐3‐3 protein in intact cells},
  author={Shinya Koyama and Lewis T. Williams and Akira Kikuchi},
  journal={FEBS Letters},
  year={1995},
  volume={368}
}
14-3-3 Antagonizes Ras-Mediated Raf-1 Recruitment to the Plasma Membrane To Maintain Signaling Fidelity
TLDR
It is shown that 14-3-3 binding, rather than Raf-1 phosphorylation, is required for the correct regulation of kinase activity, and stable association of Raf- 1 with the plasma membrane requires Ras-mediated displacement of 14- 3-3 from CR2.
Ras-interacting domain of Ral GDP dissociation stimulator like (RGL) reverses v-Ras-induced transformation and Raf-1 activation in NIH3T3 cells.
TLDR
Results clearly indicate that RID of RGL specifically binds to Ras in mammalian cells, that it blocks the signal from Ras to Raf-1, and that it reverses v-Ras-induced malignant phenotype.
14-3-3 Proteins Associate with A20 in an Isoform-specific Manner and Function Both as Chaperone and Adapter Molecules*
TLDR
The cellular localization and subcellular fractionation of A20 was dramatically altered by co-transfected 14-3-3, providing the first experimental evidence for the notion that 14- 3-3 can function as a chaperone.
Genetic networks in the mouse retina: Growth Associated Protein 43 and Phosphatase Tensin Homolog network
TLDR
The Gap43 and Pten network highlights the covariance of gene expression and forms a molecular network associated with axonal outgrowth in the adult retina and can be used to explore and test expression networks underlying variation in retina structure, function, and disease susceptibility.
Activation in NIH 3 T 3 Cells Like ( RGL ) Reverses v-Ras-induced Transformation and Raf-1 Ras-interacting Domain of Ral GDP Dissociation Stimulator
TLDR
Results clearly indicate that RID of RGL specifically binds to Ras in mammalian cells, that it blocks the signal from Ras to Raf-1, and that it reverses v-Ras-induced malignant phenotype.
Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function
TLDR
Examination of potential physical and functional interactions between PKC theta, a Ca(2+)-independent PKC enzyme which is expressed selectively in T lymphocytes, and the 14-3-3 tau isoform suggests an important general mechanism for regulating PKC-dependent signals and, more specifically, PKCTheta-mediated functions during T-cell activation.

References

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TLDR
It is concluded that 14‐3‐3 is a latent co‐activator bound to unactivated Raf‐1 in quiescent cells and mediates mitogen‐triggered but Ras‐independent regulatory effects aimed directly at the kinase domain.
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation.
TLDR
A role for 14-3-3 proteins in Raf-mediated signal transduction is suggested, which may participate in or be required for the regulation of Raf function.
Activation of Raf-1 by 14-3-3 proteins
TLDR
Using the yeast two-hybrid system, two structurally related proteins are identified that interact with the amino-terminal region of Raf-1 and are members of the 14-3-3 family of proteins.
Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
TLDR
It is reported that the amino-terminal cysteine-rich regulatory region of p74c-raf-1 expressed as a glutathione-S-transferase (GST) fusion protein binds directly to Ras with relatively high affinity (50 nM).
Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues
TLDR
A novel competition assay is used to measure in vitro the relative affinity of the c-Raf-1 regulatory region for Ras-GTP, Ras- GDP, and 10 oncogenic and effector mutant Ras proteins, demonstrating that the mechanism of cyclic AMP downregulation results through structural changes occurring exclusively in this small Ras-binding domain.
Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP.
TLDR
Four overlapping peptide fragments of human c-Raf-1 were expressed in Escherichia coli as carboxyl-terminal extensions of maltose binding protein (MBP) and showed ability to inhibit the stimulation of Ras G TPase activity by GTPase activating protein (GAP120) in vitro.
Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase.
TLDR
The forming of complexes containing MAPKK activity and Raf-1 protein are dependent upon the activity of Ras, and the specific interaction of activated Ras with active MAP kinase kinase (MAPKK) was confirmed by direct assays.
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