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The constitutive or induced re-localization of A-Raf to the plasma membrane compromises its ability to efficiently sequester and inactivate MST2, thus rendering cells susceptible to apoptosis
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This review discusses the regulation of A-Raf protein expression, and the roles of A-Raf in apoptosis and cancer, with a special focus on its role in resistance to Raf inhibitors. [review]
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analysis of FGFR2-PPHLN1 fusion and ARAF mutations in intrahepatic cholangiocarcinoma
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Aberrant expression of A-, B-, and C-RAF, and COT is frequent in PTC; increased expression of COT is correlated with recurrence of PTC.
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Dimerization of the kinase ARAF promotes MAPK pathway activation and cell migration.
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The study identifies somatic activating ARAF mutations in Langerhans cell histiocytosis.
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Galpha12-ARAF-ERK pathway stimulates RFFL transcription through the transcription factor c-Myc.
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show that Araf antagonizes mesendoderm induction and patterning activity of Nodal/Smad2 signals in vertebrate embryos by directly inhibiting Smad2 signalling
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study investigated role of ARAF in cancer cell signaling and examined the role of ARAF in mediating paradoxical activation of the MAPK pathway in cells treated with RAF inhibitors; ARAF seems to stabilize BRAF:CRAF complexes in cells treated with RAF inhibitors and regulate cell signaling in a subtle manner to ensure signaling efficiency
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Ras pathway activation via EGF treatment induced strong binding between B-Raf and C-Raf and a low level of binding between B-Raf and A-Raf.
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hnRNP H blocks MST2-mediated apoptosis in cancer cells by regulating A-Raf transcription.
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In a two-hybrid screen of human fetal liver cDNA library, TH1 was detected as a new interaction partner of A-Raf; this specific interaction may have played a critical role in the activation of A-Raf.
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A-Raf kinase is negatively regulated by trihydrophobin 1
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mutation analysis of the conserved regions in the ARAF gene in human colorectal adenocarcinoma
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A-Raf residues are identified that bind to specific phosphoinositides, possibly as a mechanism to localize the enzyme to particular membrane microdomains rich in these phospholipids.
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These data reveal that B-RAF is an important mediator of neuronal survival, migration, and dendrite formation and that A-RAF cannot fully compensate for these functions.
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Positive regulation of A-RAF by phosphorylation of isoform-specific hinge segment and identification of novel phosphorylation sites.
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A-Raf interacts with MEK1 and activates MEK1 by phosphorylation.
