RasGRP, a Ras guanyl nucleotide- releasing protein with calcium- and diacylglycerol-binding motifs

J O Ebinu, D A Bottorff, E Y Chan, S L Stang, R J Dunn, J C Stone

Research output: Contribution to journalArticlepeer-review

529 Citations (Scopus)


RasGRP, a guanyl nucleotide-releasing protein for the small guanosine triphosphatase Ras, was characterized. Besides the catalytic domain, RasGRP has an atypical pair of "EF hands" that bind calcium and a diacylglycerol (DAG)-binding domain. RasGRP activated Ras and caused transformation in fibroblasts. A DAG analog caused sustained activation of Ras-Erk signaling and changes in cell morphology. Signaling was associated with partitioning of RasGRP protein into the membrane fraction. Sustained ligand-induced signaling and membrane partitioning were absent when the DAG-binding domain was deleted. RasGRP is expressed in the nervous system, where it may couple changes in DAG and possibly calcium concentrations to Ras activation.

Original languageEnglish
Pages (from-to)1082-1086
Number of pages5
Issue number5366
Publication statusPublished - 15 May 1998


  • amino acid sequence
  • animals
  • brain
  • calcium
  • calcium-calmodulin-dependent protein kinases
  • catalysis
  • cell cycle proteins
  • cell line
  • cell membrane
  • cell size
  • cell transformation, neoplastic
  • cloning, molecular
  • DNA, complementary
  • DNA-binding proteins
  • diglycerides
  • genes, ras
  • guanine nucleotide exchange factors
  • guanosine diphosphate
  • guanosine triphosphate
  • molecular sequence data
  • neurons
  • phosphoprotein phosphatases
  • rats
  • recombinant fusion proteins
  • signal transduction
  • ras proteins
  • ras-GRF1


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