The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch (Q24313905)

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Harald Mischak

object named as

Harald Mischak

9

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author name string

Amardeep S Dhillon

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Yan Yan Yip

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G Joan Grindlay

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Julian L Pakay

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Marc Dangers

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Meike Hillmann

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William Clark

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

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language of work or name

English

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publication date

November 2009

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published in

Cellular Signalling

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volume

21

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page(s)

1645-51

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issue

11

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cites work

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CRAF autophosphorylation of serine 621 is required to prevent its proteasome-mediated degradation

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MAPK signal specificity: the right place at the right time

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14-3-3 Proteins--a focus on cancer and human disease

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Untying the regulation of the Raf-1 kinase

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How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis

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Identification of Raf-1 Ser621 kinase activity from NIH 3T3 cells as AMP-activated protein kinase

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Mechanisms of regulating the Raf kinase family

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

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Raf-1 protein kinase is required for growth of induced NIH/3T3 cells

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Regulation of the Raf-MEK-ERK pathway by protein phosphatase 5

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The RAF proteins take centre stage

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Coordinating ERK/MAPK signalling through scaffolds and inhibitors

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Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions

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14-3-3 proteins; bringing new definitions to scaffolding

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MAP kinase signalling pathways in cancer

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Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.

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

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Dephosphorylation of Ser-259 regulates Raf-1 membrane association

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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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Regulation of Raf-1 activation and signalling by dephosphorylation

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Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development.

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Gamma-phosphate-linked ATP-sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase

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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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Negative regulation of Raf-1 by phosphorylation of serine 621.

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

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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 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity

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

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14-3-3 proteins: structure, function, and regulation

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Phosphatase and feedback regulation of Raf-1 signaling

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Ras nanoclusters: combining digital and analog signaling

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