14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila.

Chang, Henry; Rubin, Gerald M.

doi:10.1101/gad.11.9.1132

Cited by 132 publications

(95 citation statements)

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“…This interaction is suppressed by a phosphorylated Raf peptide but not by its non-phosphorylated counterpart. Genetic strategies have provided strong evidence that 14-3-3 proteins, via homo-and hetero-dimeric complexes, serve as scaffolds that facilitate interactions among molecular components of signaling cascades (43,51,53). The present findings suggest that 14-3-3 proteins may play a similar role in linking G protein-coupled receptors to diverse signaling pathways by coordinating these interactions in the receptor microenvironment.…”

Section: Discussionmentioning

confidence: 55%

“…The N-terminal domains of the 14-3-3 monomers interact to form a dimer, whereas surface residues from helices 3, 5, 7, and 9 define a conserved amphipathic groove (42,46). Both charged and hydrophobic residues in this groove are involved in the interaction with several proteins, as revealed by genetic (51,52) and biochemical (45,49) analysis. For example, the Saccharomyces cerevisiae homologs of 14-3-3, BMH1 and BMH2, are essential for the Ras/ mitogen-activated protein kinase cascade during pseudohyphal development in the yeast; signaling defects due to mutations in BMH1 are not accompanied by decrements in Ras or other members of the signaling pathway but to the failure of these signaling components to interact with one another, presumably due to changes in the cleft of the amphipathic substrate binding pocket of the BMH1 mutant allele (52).…”

Section: Discussionmentioning

confidence: 99%

“…The aligned sequences for the multiple isoforms of 14-3-3 reveal the regions of considerable homology, as indicated by *. The bold type represents the peptide sequence obtained from the purified preparation of 3i loop interacting proteins, and the gray boxes indicate where this sequence is homologous to 14-3-3. development (51). It has been postulated that interaction of signaling molecules with 14-3-3 homo-or heterodimers serves as a scaffolding mechanism to facilitate interactions among molecular components of signaling cascades (42,53).…”

Section: Discussionmentioning

confidence: 99%

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The ζ Isoform of 14-3-3 Proteins Interacts with the Third Intracellular Loop of Different α2-Adrenergic Receptor Subtypes

Prézeau¹,

Richman²,

Edwards

et al. 1999

Journal of Biological Chemistry

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The ␣ 2 -adrenergic receptors (␣ 2 ARs) are localized to and function on the basolateral surface in polarized renal epithelial cells via a mechanism involving the third cytoplasmic loop. 35 S]Met-14-3-3 binds to all three native ␣ 2 AR subtypes, assessed using a solid phase binding assay (␣ 2A >␣ 2B > ␣ 2C ), and this binding depends on the presence of the 3i loops. Attenuation of the ␣ 2 AR-14-3-3 interactions in the presence of a phosphorylated Raf-1 peptide corresponding to its 14-3-3 interacting domain (residues 251-266), but not by its non-phosphorylated counterpart, provides evidence for the functional specificity of these interactions and suggests one potential interface for the ␣ 2 AR and 14-3-3 interactions. These studies represent the first evidence for G protein-coupled receptor interactions with 14-3-3 proteins and may provide a mechanism for receptor localization and/or coordination of signal transduction.The three ␣ 2 -adrenergic receptor (␣ 2 AR) 1 subtypes, encoded by distinct genes (1), all couple via the G i /G o family of GTPbinding proteins to inhibition of adenylyl cyclase, suppression of voltage-sensitive calcium channels, and activation of receptor-operated potassium channels (2). These receptors also couple to activation of Ras (3, 4), the mitogen-activated protein kinase cascade (3, 5-7), and to activation of phospholipase D (8, 9).Despite the qualitatively similar signaling properties of the three ␣ 2 AR subtypes, differences in trafficking of these receptors have been reported. For example, subtype-selective differences in agonist-elicited ␣ 2 AR redistribution occur (10 -15). In addition, selective itineraries for the ␣ 2 AR subtypes are observed in polarized Madin-Darby canine kidney (MDCKII) renal epithelial cells. Thus, the ␣ 2A AR subtype is targeted directly to the basolateral surface (16), whereas the ␣ 2B AR subtype is delivered randomly to both the apical and basolateral surfaces but is rapidly lost from the apical (t1 ⁄2 ϭ 5-15 min) and selectively retained on the basolateral (t1 ⁄2 ϭ 10 -12 h) surface (17). These findings suggest that there is a molecular mechanism responsible for the selective retention of the ␣ 2B AR on the basolateral domain of MDCK cells that may be shared by all three ␣ 2 AR subtypes, as they manifest comparable halflives on that surface (17).Receptor retention on the lateral subdomain of MDCKII cells likely involves the third intracellular loop of the ␣ 2A AR, since deletion of this loop, creating the mutant ␣ 2A ⌬3iAR, results in accelerated basolateral turnover (t1 ⁄2 Х 4.5 h) when compared with that for the wild-type receptor or with ␣ 2A AR structures that have been mutated in the N terminus or the C-terminal tail (all possessing a t1 ⁄2 of 10 -12 h) (18). The accelerated turnover of the ␣ 2A ⌬3iAR when compared with the wild-type ␣ 2A AR structure suggests that the third intracellular loop interacts with proteins that either tether ␣ 2A AR to a particular surface domain or, alternatively, mask the ␣ 2A AR from interacting with endocytosis machiner...

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Section: Discussionmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The ζ Isoform of 14-3-3 Proteins Interacts with the Third Intracellular Loop of Different α2-Adrenergic Receptor Subtypes

Prézeau¹,

Richman²,

Edwards

et al. 1999

Journal of Biological Chemistry

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“…Another molecule identified in our screen is the zeta isoform of the 14-3-3 family of proteins, which are key regulators and integrators of many different signal transduction pathways, and mediate such diverse cellular processes as proliferation, differentiation, survival, and apoptosis (Skoulakis and Davis, 1998;Fu et al, 2000). Of interest, they are abundantly expressed in the nervous system and disruptions in their function perturb neuronal differentiation (Chang and Rubin, 1997;Kockel et al, 1997;Li et al, 1996;Skoulakis and Davis, 1998). For example, disruption of 14-3-3 binding to the B-Raf kinase domain uncouples NGF induced cellular differentiation of PC12 cells (MacNicol et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Identification of genes regulating sensory neuron genesis and differentiation in the avian dorsal root ganglia

Nelson

Sadhu

Kasemeier

et al. 2004

Developmental Dynamics

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The dorsal root ganglia (DRG) derive from a population of migrating neural crest cells that coalesce laterally to the neural tube. As the DRG matures, discrete cell types emerge from a pool of differentiating progenitor cells. To identify genes that regulate sensory genesis and differentiation, we have designed screens to identify members from families of known regulatory molecules such as receptor tyrosine kinases, and generated full-length and subtractive cDNA libraries between immature and mature DRG for identifying novel genes not previously implicated in DRG development. Several genes were identified in these analyses that belong to important regulatory gene families. Quantitative PCR confirmed differential expression of candidate cDNAs identified from the subtraction/differential screening. In situ hybridization further validated dynamic expression of several cDNAs identified in our screens. Our results demonstrate the utility of combining specific and general screening approaches for isolating key regulatory genes involved in the genesis and differentiation of discrete cell types and tissues within the classic embryonic chick model system. Developmental Dynamics 229:618 -629, 2004.

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“…Cependant, les protéines 14-3-3 n'agissent pas uniquement comme antagonistes : leur liaison à l'extrémité carboxy-terminale de RAF est également essentielle pour l'activité catalytique de ce dernier [39]. En accord avec ces rôles-clés, deux études génétiques chez la mouche ont validé l'importance fonctionnelle des protéines 14-3-3 comme régulateurs de l'activité de RAF [40,41]. Par ailleurs, des analyses génétiques de la sous-unité catalytique (LET-92) et régulatrice B (SUR-6) de PP2A chez le nématode ont aussi confirmé l'importance de cette activité phosphatase pour réguler RAF et KSR [42,43].…”

Section: Apport Des Modèles Génétiquesunclassified

La signalisation RTK/RAS/ERK élargie

Ashton‐Beaucage

Therrien

2010

Med Sci (Paris)

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14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila.

Cited by 132 publications

References 59 publications

The ζ Isoform of 14-3-3 Proteins Interacts with the Third Intracellular Loop of Different α2-Adrenergic Receptor Subtypes

The ζ Isoform of 14-3-3 Proteins Interacts with the Third Intracellular Loop of Different α2-Adrenergic Receptor Subtypes

Identification of genes regulating sensory neuron genesis and differentiation in the avian dorsal root ganglia

La signalisation RTK/RAS/ERK élargie

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