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Structural basis for ligand-mediated mouse GITR activation.

Zhaocai Zhou1, Yukiko Tone, Xiaomin Song

  • 1Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 8, 2008
PubMed
Summary
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Mouse GITRL, a TNF super family ligand, uniquely forms dimers, not trimers. This dimer is biologically active and influences regulatory T cell signaling.

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Glucocorticoid-induced TNF receptor ligand (GITRL) is a key regulator of T cell responses.
  • Members of the TNF super family (TNFSF) typically form trimers, influencing receptor interactions.

Purpose of the Study:

  • To determine the oligomeric state and structure of mouse GITRL (mGITRL).
  • To investigate the biological activity and signaling implications of different mGITRL oligomeric forms.

Main Methods:

  • X-ray crystallography to determine mGITRL structure.
  • Analytical ultracentrifugation to assess oligomeric states in solution.
  • Biochemical assays to evaluate receptor-mediated signaling.

Main Results:

Related Experiment Videos

  • Mouse GITRL (mGITRL) crystallizes as a dimer, challenging the TNFSF trimer paradigm.
  • Recombinant mGITRL exists as monomers at low and dimers at high concentrations in solution.
  • The mGITRL dimer is biologically active, with modifications to the C-terminus affecting NF-kappaB activation.

Conclusions:

  • mGITRL exhibits dynamic oligomerization via its C-terminus, shifting between monomeric and dimeric forms.
  • Specific oligomeric states of GITRL may differentially regulate GITR receptor signaling in various cell types.