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Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from ras to

J Settleman1, V Narasimhan, L C Foster

  • 1Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.

Cell
|May 1, 1992
PubMed

Insights

Researchers identified a protein, p190, that complexes with ras GTPase-activating protein (GAP) in stimulated cells. This protein has domains suggesting roles in GTPase regulation and transcriptional repression, potentially linking ras signaling to nuclear gene expression.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Genetics

Background:

  • Ras GTPase-activating protein (GAP) plays a crucial role in regulating ras signaling pathways.
  • p190 protein has been observed to form complexes with ras GAP in stimulated and transformed cells.

Purpose of the Study:

  • To clone and characterize the p190 protein.
  • To elucidate the functional domains and potential roles of p190 in cellular signaling.

Main Methods:

  • Cloning of complementary DNAs (cDNAs) encoding the p190 protein.
  • Bioinformatic analysis of the predicted protein sequence to identify homologous domains.

Main Results:

  • The p190 protein sequence contains three distinct domains with significant homology to known proteins.
  • An N-terminal domain shows homology to GTPase motifs.
  • The C-terminal domain is similar to known GAP proteins, and a central domain is homologous to a transcriptional repressor.

Conclusions:

  • p190 possesses structural features suggesting dual functionality in GTPase regulation and transcriptional repression.
  • p190 may act as a signaling mediator, transducing signals from ras GTPase-activating protein to the nucleus.
  • This interaction could influence the expression of specific cellular genes, impacting cellular processes.

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