Identification of a mouse orthologue of the human ras-GAP-SH3-domain binding protein and structural confirmation that these proteins contain an RNA recognition motif

Biomed Pept Proteins Nucleic Acids. 1996;2(3):93-9.

Abstract

Human ras-GTPase-activating protein (GAP120) SH3-domain-binding protein (G3BP) has recently been identified on the basis of its specific binding to the GAP120 SH3 binding domain. Here we report the identification of a mouse G3BP cDNA and the confirmation by three dimensional modelling of an RNA recognition motif (RRM) in the encoded protein. Mouse G3BP also contains an RGG domain, an acid-rich amino acid domain, and several SH3 domain-binding consensus sequences, indicating that mammalian G3BPs represent a new family of signal transduction proteins which connect tyrosine kinase-linked receptors to cellular RNA metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • DNA Primers / genetics
  • DNA, Complementary / genetics
  • GTPase-Activating Proteins
  • Humans
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Ribonucleoprotein, U1 Small Nuclear / chemistry
  • Ribonucleoprotein, U1 Small Nuclear / genetics
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Species Specificity
  • ras GTPase-Activating Proteins
  • src Homology Domains

Substances

  • DNA Primers
  • DNA, Complementary
  • GTPase-Activating Proteins
  • Proteins
  • RNA-Binding Proteins
  • Ribonucleoprotein, U1 Small Nuclear
  • U1A protein
  • ras GTPase-Activating Proteins
  • RNA