Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins

J Mol Med (Berl). 1999 Oct;77(10):695-8. doi: 10.1007/s001099900054.


Ras proteins play critical roles in regulating cell growth and differentiation, and mutated Ras genes are expressed in a variety of human cancers. Consequently, much interest has centered on the binding partners of Ras, including the Ras-binding domain (RBD) of Raf kinase. Here evidence is presented that domains homologous to the Raf RBD are present in tandem in RGS12, RGS14 and LOCO, and singly in molecules similar to mouse Tiam-1. In addition, RGS12, RGS14 and LOCO are shown to contain single "LGN motifs" that are guanine nucleotide exchange factors specific for the alpha-subunit of G proteins. These findings indicate "cross-talk" interactions between signalling pathways involving Ras and Rap and pathways involving Rho, Rac and G alpha GTPases.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animal Population Groups / genetics
  • Animals
  • Consensus Sequence
  • GTPase-Activating Proteins / metabolism
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins c-raf / chemistry
  • RGS Proteins / chemistry*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Signal Transduction*
  • Species Specificity
  • ras Proteins / metabolism


  • GTPase-Activating Proteins
  • RGS Proteins
  • RGS12 protein, human
  • Proto-Oncogene Proteins c-raf
  • ras Proteins