Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins (Q24320264)

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English	Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins	scientific article

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scholarly article

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Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins (English)

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2

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author name string

Andreas Fischer

1

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Joerg Reinders

3

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Elena Nekhoroshkova

4

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Claudia Sibilski

5

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Renate Metz

6

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Stefan Albert

7

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Krishnaraj Rajalingam

8

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Mirko Hekman

9

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Ulf R Rapp

10

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language of work or name

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publication date

30 January 2009

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Journal of Biological Chemistry

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284

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3183-94

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5

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The RAF proteins take centre stage

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Structure and biological activity of human homologs of the raf/mil oncogene

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Characterization of murine A-raf, a new oncogene related to the v-raf oncogene

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95-kilodalton B-Raf serine/threonine kinase: identification of the protein and its major autophosphorylation site

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B- and C-RAF display essential differences in their binding to Ras: the isotype-specific N terminus of B-RAF facilitates Ras binding

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Unique N-region determines low basal activity and limited inducibility of A-RAF kinase: the role of N-region in the evolutionary divergence of RAF kinase function in vertebrates

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Signal transduction from membrane to cytoplasm: growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity

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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF

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A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity

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Dynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sites

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Phosphorylation and regulation of Raf by Akt (protein kinase B)

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Regulation of Raf-1 activation and signalling by dephosphorylation

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Regulation of Raf-Akt Cross-talk

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Dephosphorylation of Ser-259 regulates Raf-1 membrane association

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Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants

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Unlocking the code of 14-3-3.

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Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein.

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Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo

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14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation

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Proteomic analysis of in vivo 14-3-3 interactions in the yeast Saccharomyces cerevisiae.

1 reference

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Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras.

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14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain

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NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation

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The ins and outs of Raf kinases

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Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: preferential binding of Raf to artificial lipid rafts.

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Cyclic AMP-dependent kinase regulates Raf-1 kinase mainly by phosphorylation of serine 259.

1 reference

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Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites

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Prohibitin is required for Ras-induced Raf-MEK-ERK activation and epithelial cell migration

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Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization

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Regulation and role of Raf-1/B-Raf heterodimerization

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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

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Dynamic 14-3-3/client protein interactions integrate survival and apoptotic pathways.

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Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms

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14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo

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Bcl-2 targets the protein kinase Raf-1 to mitochondria

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The protein kinase KSR interacts with 14-3-3 protein and Raf.

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Mutations of C-RAF are rare in human cancer because C-RAF has a low basal kinase activity compared with B-RAF

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