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Ras-interacting domain of RGL blocks Ras-dependent signal transduction in Xenopus oocytes

S Koyama1, Y W Chen, M Ikeda

  • 1Department of Biochemistry, Hiroshima University School of Medicine, Japan.

FEBS Letters
|February 12, 1996
PubMed

Insights

Researchers identified a minimal Ras-interacting domain within RGL (amino acids 632-734) crucial for Ras-dependent signaling. This domain inhibits Ras-GTP binding and downstream signaling in Xenopus oocytes.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Ras Pathway Research

Background:

  • RalGDS family members, including RGL, interact with GTP-bound Ras.
  • The C-terminal region of RGL (amino acids 602-768) is known to bind Ras.

Purpose of the Study:

  • To characterize the Ras-interacting domain of RGL using deletion mutants.
  • To determine the minimal domain responsible for Ras binding and downstream signaling inhibition.

Main Methods:

  • Construction and testing of RGL deletion mutants (RGL(602-768), RGL(632-768), RGL(602-734), RGL(646-768), RGL(659-768), RGL(685-768), RGL(602-709), RGL(602-686)).
  • Assays for Ras binding and inhibition of NF-1 GTPase-activating protein (GAP) activity.
  • Xenopus oocyte maturation and extracellular signal-regulated kinase (ERK) activation assays.

Main Results:

  • Amino acids 632-734 of RGL form a nearly minimal domain for Ras binding.
  • This domain (RGL(632-734)) inhibited Ras-GTP binding and NF-1 GAP activity.
  • RGL(632-734) specifically inhibited v-Ras-induced Xenopus oocyte maturation and ERK activation, but not progesterone-induced maturation or v-Raf-dependent ERK activation.

Conclusions:

  • The identified Ras-interacting domain (amino acids 632-734) is essential for Ras binding.
  • This domain plays a critical role in Ras-dependent signal transduction pathways in vivo.

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