14-3-3 Facilitates Ras-Dependent Raf-1 Activation In Vitro and In Vivo

No abstract is available for this paper.

• Publication year

  1998

• Venue

  Molecular and Cellular Biology

• Publication date

  1998-07-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1128/MCB.18.7.3947PMID 9632779PMCID PMC108979
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Activation mechanism of the MAP kinase ERK2 by dual phosphorylation.

  1997cited by this paper
• The complexity of Raf-1 regulation.

  1997cited by this paper
• Differential Regulation of Raf-1, A-Raf, and B-Raf by Oncogenic Ras and Tyrosine Kinases*

  1997cited by this paper
• 14-3-3 ζ Negatively Regulates Raf-1 Activity by Interactions with the Raf-1 Cysteine-rich Domain*

  1997influential reference
• Activity of Plasma Membrane-recruited Raf-1 Is Regulated by Ras via the Raf Zinc Finger*

  1997cited by this paper
• Activation of c‐Raf‐1 by Ras and Src through different mechanisms: activation in vivo and in vitro

  1997cited by this paper
• Sequential Modification of Serines 621 and 624 in the Raf-1 Carboxyl Terminus Produces Alterations in Its Electrophoretic Mobility*

  1997cited by this paper
• Physical Association with Ras Enhances Activation of Membrane-bound Raf (RafCAAX)*

  1997cited by this paper
• 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila.

  1997cited by this paper
• Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development.

  1997cited by this paper
• Negative Modulation of Membrane Localization of the Raf-1 Protein Kinase by Hyperphosphorylation*

  1997cited by this paper
• An intact Raf zinc finger is required for optimal binding to processed Ras and for ras-dependent Raf activation in situ

  1997cited by this paper
• Negative regulation of Raf activity by binding of 14-3-3 to the amino terminus of Raf in vivo.

  1997influential reference
• Activated Ras displaces 14-3-3 protein from the amino terminus of c-Raf-1.

  1996cited by this paper
• Raf-1 Kinase Possesses Distinct Binding Domains for Phosphatidylserine and Phosphatidic Acid

  1996cited by this paper
• Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization

  1996cited by this paper
• Oligomerization activates c-Raf-1 through a Ras-dependent mechanism

  1996cited by this paper
• KSR modulates signal propagation within the MAPK cascade.

  1996cited by this paper
• Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.

  1996influential reference
• Negative regulation of Raf-1 by phosphorylation of serine 621

  1996cited by this paper
• Protein Kinase C δ Activates the MEK-ERK Pathway in a Manner Independent of Ras and Dependent on Raf*

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• Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation

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• Inhibition of Raf/MAPK signaling in Xenopus oocyte extracts by Raf-1-specific peptides.

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• Control of the ERK MAP kinase cascade by Ras and Raf.

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• Ras Interaction with Two Distinct Binding Domains in Raf-1 5 Be Required for Ras Transformation (*)

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• Two Distinct Raf Domains Mediate Interaction with Ras (*)

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• Cysteine-rich Region of Raf-1 Interacts with Activator Domain of Post-translationally Modified Ha-Ras (*)

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• Regulation of Raf‐1 kinase activity by the 14‐3‐3 family of proteins.

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• Identification of the 14.3.3 ζ Domains Important for Self-association and Raf Binding (*)

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• Lack of evidence for the activation of the Ras/Raf mitogenic pathway by 14-3-3 proteins in mammalian cells.

  1995cited by this paper
• Ras recruits Raf‐1 to the plasma membrane for activation by tyrosine phosphorylation.

  1995influential reference
• Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation.

  1995cited by this paper
• 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner

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• Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells.

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  1994cited by this paper
• Activation of Raf as a result of recruitment to the plasma membrane.

  1994cited by this paper
• Interaction of the protein kinase Raf-1 with 14-3-3 proteins.

  1994cited by this paper
• Activation of Raf-1 by 14-3-3 proteins

  1994cited by this paper
• The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras.

  1994cited by this paper
• Identification of discrete segments of human Raf-1 kinase critical for high affinity binding to Ha-Ras.

  1994cited by this paper
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  1994cited by this paper
• Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase.

  1994cited by this paper
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  1993cited by this paper
• Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro

  1993cited by this paper
• A novel role for RhoGDI as an inhibitor of GAP proteins.

  1993cited by this paper
• Requirement for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytes

  1993cited by this paper
• Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

  1993cited by this paper
• Mammalian Ras interacts directly with the serine/threonine kinase Raf.

  1993cited by this paper
• Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase

  1993cited by this paper
• Identification of the major phosphorylation sites of the Raf-1 kinase.

  1993cited by this paper
• Specific association of activated MAP kinase kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells.

  1993cited by this paper

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