Evidence for a Ras/Ral signaling cascade.
It is becoming clear that Ras proteins mediate their diverse biological functions by binding to, and participating in, the activation of multiple downstream targets. Recent work has identified nucleotide-exchange factors for Ral-GTPases as the newest members of the set of putative Ras 'effector molecules'. This new work has also detected two potential downstream targets of Ral proteins, a novel CDC42/Rac GTPase-activating protein and a phospholipase D.
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Department of Biochemistry, Sackler School of Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111, USA. ifeig@opal.tufts.edu
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D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D010739:Phospholipase D / Q000378:metabolism*; D015398:Signal Transduction; D020846:cdc42 GTP-Binding Protein, Saccharomyces cerevisiae; D020744:rac GTP-Binding Proteins; D020668:rap GTP-Binding Proteins; D018631:ras Proteins / Q000378:metabolism*
D018797:Cell Cycle Proteins; D010739:Phospholipase D; D019204:GTP-Binding Proteins; D020846:cdc42 GTP-Binding Protein, Saccharomyces cerevisiae; D020744:rac GTP-Binding Proteins; D020668:rap GTP-Binding Proteins; D018631:ras Proteins