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SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins

S C Borinstein1, M A Hyatt, V W Sykes

  • 1Department of Anatomy, Medical College of Virginia, Virginia Commonwealth University, Richmond, VA 23298, USA.

Cellular Signalling
|January 12, 2001
PubMed

Insights

The SETA gene, linked to astrocyte tumors, has an additional SH3 domain. This domain helps identify a new binding protein, SB1, which interacts with SETA and influences astrocyte apoptosis.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Neuroscience

Background:

  • The src homology 3 (SH3)-encoding, expressed in tumorigenic astrocytes (SETA) gene is implicated in astrocyte transformation and brain tumors.
  • SETA interacts with apoptosis regulator AIP1, modulating astrocyte apoptosis.
  • Previous structural analysis indicated two SH3 domains in SETA, contrary to related proteins with three.

Purpose of the Study:

  • To identify novel proteins interacting with SETA.
  • To characterize the function of SETA and its binding partners in astrocyte biology.
  • To investigate the role of SETA in tumorigenesis.

Main Methods:

  • Yeast two-hybrid screening of a p53(-/-) astrocyte cDNA library.
  • In vitro confrontation assays.
  • Co-immunoprecipitation experiments.

Main Results:

  • An additional N-terminal SH3 domain was identified in SETA.
  • A novel gene, SETA binding protein 1 (SB1), was identified through yeast two-hybrid screening.
  • SB1 demonstrated 55% amino acid identity to the renal tumor antigen NY-REN-45.
  • Binding of SB1 to SETA was confirmed via in vitro and co-immunoprecipitation experiments.
  • SETA was shown to bind CD2, c-Cbl, and Grb2, and to dimerize via its C-terminal coiled coil domain.

Conclusions:

  • The discovery of an additional SH3 domain in SETA expands our understanding of its structure.
  • SB1 is a novel SETA-binding protein with potential roles in astrocyte biology and tumorigenesis.
  • SETA's interactions with multiple proteins suggest a role in complex signaling pathways relevant to cancer.

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