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The lymphocyte receptor CD6 interacts with syntenin-1, a scaffolding protein containing PDZ domains

Idoia Gimferrer1, Anna Ibáñez, Montse Farnós

  • 1Servei d'Immunologia, Hospital Clínic Universitari, Institut di Investigacions Biomèdiques August Pi i Sunyer, Facultat de Medicina, Universitat de Barcelona, Barcelona, Spain.

Journal of Immunology (Baltimore, Md. : 1950)
|July 22, 2005
PubMed

Insights

Researchers identified syntenin-1 as a binding partner for CD6, a T cell costimulatory molecule. This interaction is crucial for scaffolding CD6 and other receptors at the immunological synapse, impacting lymphocyte activation.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • CD6 is a T cell costimulatory molecule involved in lymphocyte activation and development.
  • The signaling pathway of CD6, particularly its role in the immunological synapse (IS), remains largely uncharacterized.

Purpose of the Study:

  • To identify proteins interacting with the cytoplasmic tail of CD6.
  • To elucidate the role of CD6-interacting proteins in T cell signaling and IS formation.

Main Methods:

  • Yeast two-hybrid screening to identify CD6 interacting partners.
  • Mutational analysis to define key interaction domains between CD6 and syntenin-1.
  • Pull-down assays, co-immunoprecipitation, and imaging to confirm and visualize the interaction in mammalian cells.

Main Results:

  • Syntenin-1 was identified as a direct interacting protein of the CD6 cytoplasmic tail.
  • Specific amino acids in CD6 and PDZ domains of syntenin-1 are critical for their interaction.
  • Syntenin-1 was shown to accumulate at CD6 caps and the immunological synapse.

Conclusions:

  • Syntenin-1 acts as a scaffolding protein, linking CD6 to the cytoskeleton and signaling molecules.
  • This interaction is important for the maturation of the immunological synapse and T cell activation.

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