Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins (Q28142961)

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S Zhuang

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F C von Lintig

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G R Boss

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R B Pilz

Journal of Biological Chemistry

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language of work or name

English

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publication date

13 October 2000

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published in

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volume

275

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issue

41

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page(s)

31921-9

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cites work

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Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH 3T3 cells

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

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Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

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Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation

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Modulation of kinase activity and oncogenic properties by alternative splicing reveals a novel regulatory mechanism for B-Raf

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Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells

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Suppression of Ras-induced transformation of NIH 3T3 cells by activated G alpha s.

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Inhibitors of cyclic nucleotide phosphodiesterase isozymes type-III and type-IV suppress mitogenesis of rat mesangial cells

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cAMP activates MAP kinase and Elk-1 through a B-Raf- and Rap1-dependent pathway

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Increasing cAMP attenuates activation of mitogen-activated protein kinase

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Parathyroid hormone activates mitogen-activated protein kinase via a cAMP-mediated pathway independent of Ras.

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A family of cAMP-binding proteins that directly activate Rap1

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

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14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity

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

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

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

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Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins

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Signal transduction pathways regulated by mitogen-activated/extracellular response kinase kinase kinase induce cell death

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Cyclic-GMP-dependent protein kinase inhibits the Ras/Mitogen-activated protein kinase pathway

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Assay for nanogram quantities of DNA in cellular homogenates

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Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling

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The mouse B-raf gene encodes multiple protein isoforms with tissue-specific expression.

21 January 2018

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Activity of Rap1 is regulated by bombesin, cell adhesion, and cell density in NIH3T3 fibroblasts

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Differential effects on cAMP on the MAP kinase cascade: evidence for a cAMP-insensitive step that can bypass Raf-1

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Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein

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14-3-3 proteins block apoptosis and differentially regulate MAPK cascades

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Nerve Growth Factor-mediated Activation of the Mitogen-activated Protein (MAP) Kinase Cascade Involves a Signaling Complex Containing B-Raf and HSP90

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