Raf-1: A kinase currently without a cause but not lacking in effects

  title={Raf-1: A kinase currently without a cause but not lacking in effects},
  author={Ping Li and Kenneth W. Wood and Harvey J. Mamon and Wayne G. Haser and Tom Roberts},
Negative Modulation of Membrane Localization of the Raf-1 Protein Kinase by Hyperphosphorylation*
It is shown that incubation of serum-starved CHO cells with D609, a purported inhibitor of phosphatidylcholine-specific phospholipase C, results in a mobility shift of Raf-1 that is due to hyperphosphorylation on sites identical to those observed following mitogen stimulation, suggesting a negative feedback mechanism contributing to the desensitization of the MAP kinase signaling cascade.
Signal transduction pathways involving the raf proto-oncogene
Accumulating evidence indicates that membrane tyrosine kinases, ras, Raf-1, MEK and MAP kinase are interconnected via a complex network rather than via a linear pathway involving multiple substrates and feedback loops.
Raf functions downstream of Rasl in the Sevenless signal transduction pathway
It is shown that the Drosophila Raf serine/threonine kinase also plays a crucial role in the R7 pathway: the response to Sev activity is dependent on raf function, and a constitutively activated Raf protein can induce R7 cell development in the absence of sev function.
The MAP kinase cascade. Discovery of a new signal transduction pathway
  • N. Ahn
  • Biology
    Molecular and Cellular Biochemistry
  • 2005
Preliminary findings suggesting multiple feedback or feedforward regulation of several components in the cascade predict higher complexity than a simple linear pathway.
Sequential Modification of Serines 621 and 624 in the Raf-1 Carboxyl Terminus Produces Alterations in Its Electrophoretic Mobility*
It is demonstrated that treatment of NIH 3T3 cells or Sf9 cells with hydrogen peroxide also induces the mobility shift of the kinase-inactive Raf-1 fragment, and co-expression of the 33-kDa fragment with an activated form of mitogen-activated protein kinase kinase in NIH3T3 led to the appearance of the shifted form in a serum-independent manner.
Biochemical analysis of torso and D-raf during Drosophila embryogenesis: implications for terminal signal transduction
This report provides the first biochemical analysis of the terminal signal transduction pathway in Drosophila embryos, demonstrating that Torso has intrinsic tyrosine kinase activity and that it is transiently tyosine phosphorylated (activated) at syncytial blastoderm stages.


Relationship of a putative receptor protein kinase from maize to the S-locus glycoproteins of Brassica
A complementary DNA clone from Zea mays (L.) is identified encoding a putative serine/threonine-specific protein kinase structurally related to the receptor tyrosine kinases, evidence for a previously undescribed class of transmembrane receptor in higher plants likely to be involved in signal reception and transduction.
Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
It is demonstrated that MAP kinase is only active when both tyrosyl and threonyl residues are phosphorylated and suggested therefore that the enzyme functions in vivo to integrate signals from two distinct transduction pathways.
Requirement for c-ras proteins during viral oncogene transformation
The results show that transformation by three growth factor receptor-like oncogenes depends on c-ras proteins, while transformation by two cytoplasmic onCogenes appears to be independent ofc-ras protein.
Colony stimulating factor‐1 (CSF‐1) stimulates temperature dependent phosphorylation and activation of the RAF‐1 proto‐oncogene product.
While RAF‐1 is not a direct substrate for the CSF‐1 receptor tyrosine kinase in vivo, its temperature dependent phosphorylation and activation represent an intriguing aspect of the CSf‐1 response.
Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-gamma in quiescent BALB/c 3T3 cells.
Results suggest that mitogenic signaling by PDGF is coincident with tyrosine phosphorylation of PLC-gamma, a key enzyme of the phosphoinositide pathway believed to be an important site for hormonal regulation of the hydrolysis of phosphatidylinositol 4,5-bisphosphate, which produces the intracellular second-messenger molecules inositol 1,2-diacylglycerol.