title: Evidence for a Ras/Ral signaling cascade.
abstract: 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.
authors.affiliation: Department of Biochemistry, Sackler School of Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111, USA. ifeig@opal.tufts.edu
authors.forename: L A
authors.initials: LA
authors.lastname: Feig
authors.forename: T
authors.initials: T
authors.lastname: Urano
authors.forename: S
authors.initials: S
authors.lastname: Cantor
mesh_terms: 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*
chemical_list: 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