IndraLab

"Phosphorylation. Raf is principally activated by phosphorylation of specific amino acid residues as shown for each isoform in Figure 4. From an evolutionary standpoint, the Raf activation sites are highly conserved from yeast to humans. Several amino acids in Raf, particularly serine (S) 259 and S621, which bind 14-3-3 and maintain C-Raf in a closed auto-inhibited conformation, are phosphorylated in the basal state."

"the phosphorylation of Raf-1 on Ser-259 induced by paclitaxel he region surrounding Ser-259 in Raf-1 conforms to a consensus sequence for phosphorylation by Akt"

"Raf itself is negatively regulated by phosphorylation at Ser259 through Akt, an important effector of phosphoinositide 3-kinase (PI3K) signaling (30, 44)."

"This zinc-induced protein kinase A activation inhibited Raf-1 activity by phosphorylation at serine 259, preventing activation of Raf-1 by phosphorylation of serine 338."

"The cyclic AMP (cAMP)-dependent protein kinase (PKA) can inhibit Raf-1 by direct phosphorylation. We have mapped all cAMP-induced phosphorylation sites in Raf-1, showing that serines 43, 259, and 621 are phosphorylated by PKA in vitro and induced by cAMP in vivo."

"This inhibitory phosphorylation on Raf reduces the activity of MAPK pathway (Zimmermann and Moelling, 1999)."

"Phosphorylation. Raf is principally activated by phosphorylation of specific amino acid residues as shown for each isoform in Figure 4. From an evolutionary standpoint, the Raf activation sites are highly conserved from yeast to humans. Several amino acids in Raf, particularly serine (S) 259 and S621, which bind 14-3-3 and maintain C-Raf in a closed auto-inhibited conformation, are phosphorylated in the basal state."

"the phosphorylation of Raf-1 on Ser-259 induced by paclitaxel he region surrounding Ser-259 in Raf-1 conforms to a consensus sequence for phosphorylation by Akt"

"The cyclic AMP (cAMP)-dependent protein kinase (PKA) can inhibit Raf-1 by direct phosphorylation. We have mapped all cAMP-induced phosphorylation sites in Raf-1, showing that serines 43, 259, and 621 are phosphorylated by PKA in vitro and induced by cAMP in vivo. "

"Phosphorylation. Raf is principally activated by phosphorylation of specific amino acid residues as shown for each isoform in Figure 4. From an evolutionary standpoint, the Raf activation sites are highly conserved from yeast to humans. Several amino acids in Raf, particularly serine (S) 259 and S621, which bind 14-3-3 and maintain C-Raf in a closed auto-inhibited conformation, are phosphorylated in the basal state.137 On stimulation, Ras-GTP displaces 14-3-3 from S259, and C-Raf is translocated to the cell membrane, where it can be dephosphorylated at S259 by protein phosphatase 2A or other phosphatases.126 S259 also represents the site of inhibitory phosphorylation by PKB/Akt, PKA, and serum glucocorticoid-inducible kinase.121,138,139 Phosphorylation at S621 seems to have greater significance because mutations at this site inactivate Raf's kinase activity. Hence, a balance of phosphorylation and dephosphorylation is required to prime Raf in the basal state before stimulation by Ras or mitogens.137"

"Raf itself is negatively regulated by phosphorylation at Ser259 through Akt, an important effector of phosphoinositide 3-kinase (PI3K) signaling (30, 44)."

"This inhibitory phosphorylation on Raf reduces the activity of MAPK pathway (Zimmermann and Moelling, 1999)."

"This zinc-induced protein kinase A activation inhibited Raf-1 activity by phosphorylation at serine 259, preventing activation of Raf-1 by phosphorylation of serine 338. "