Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo.

M K Jones, J H Jackson
Author Information
  1. M K Jones: Scripps Research Institute, La Jolla, California 92037, USA.

Abstract

Human cells contain four homologous Ras proteins, but it is unknown whether these homologues have different biological functions. As a first step in determining if Ras homologues might participate in distinct signaling cascades, we assessed whether a given Ras guanine nucleotide exchange factor could selectively activate a single Ras homologue in vivo. We found that Ras-GRF/Cdc25Mm activates Ha-Ras, but does not activate N-Ras or K-Ras 4B, protein in vivo. Moreover, our results suggested that residues within the C-terminal hypervariable domains of Ras proteins may dictate, at least in part, the specificity of Ras-GRF/CDC25Mm for Ha-Ras protein. Our studies represent the first biochemical evidence that a Ras GEF can selectively activate a single Ras homologue in vivo. Selective activation of a single Ras homologue by Ras-GRF/Cdc25Mm or other Ras guanine nucleotide exchange factors could potentially enable each of the Ras homologues to participate in different signal transduction pathways.

Grants

  1. CA-54298/NCI NIH HHS

MeSH Term

3T3 Cells
Amino Acid Sequence
Animals
Cell Cycle Proteins
Cell Line
Eukaryotic Initiation Factor-2
GTP-Binding Proteins
Genes, ras
Guanine Nucleotide Exchange Factors
Humans
Mice
Molecular Sequence Data
Phosphoprotein Phosphatases
Proteins
ras Guanine Nucleotide Exchange Factors
ras Proteins
ras-GRF1

Chemicals

Cell Cycle Proteins
Eukaryotic Initiation Factor-2
Guanine Nucleotide Exchange Factors
Proteins
ras Guanine Nucleotide Exchange Factors
ras-GRF1
Phosphoprotein Phosphatases
GTP-Binding Proteins
ras Proteins

Word Cloud

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