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

Julius Ebinu, Drell A. Bottorff, Edmond Y.W. Chan, Stacey L. Stang, Robert J. Dunn, James C. Stone

Research output: Contribution to journalArticlepeer-review

540 Scopus citations

Abstract

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 (US)
Pages (from-to)1082-1086
Number of pages5
JournalScience
Volume280
Issue number5366
DOIs
StatePublished - May 15 1998
Externally publishedYes

ASJC Scopus subject areas

  • General

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