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Subunit interactions influence TSHR multimerization.

Rauf Latif1, Krzysztof Michalek, Terry F Davies

  • 1Mount Sinai School of Medicine, James J. Peters Veterans Affairs Medical Center, New York, New York 10468, USA. rauf.latif@mssm.edu

Molecular Endocrinology (Baltimore, Md.)
|August 20, 2010
PubMed
Summary
This summary is machine-generated.

Thyroid-stimulating hormone receptor (TSHR) β-subunits interact with full-length TSHRs, decreasing cell surface expression and impairing TSH signaling. This multimerization influences TSHR internalization and function.

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Area of Science:

  • Endocrinology
  • Molecular Cell Biology

Background:

  • The TSH receptor (TSHR) is crucial for thyroid function and a target in autoimmune thyroid diseases.
  • TSHR exists in various forms due to intramolecular cleavage, producing α- and β-subunits.
  • Cleaved TSHR forms, particularly β-subunits, can affect cell surface expression and signaling.

Purpose of the Study:

  • To model the influence of cleaved TSHR β-subunits on full-length TSHR cell surface expression and signaling.
  • To investigate the interaction and functional consequences of truncated β-subunits with wild-type TSHR.

Main Methods:

  • Generated truncated TSHR β-subunits (β-316, -366, -409) linked to GFP.
  • Expressed these constructs with full-length TSHR in HEK293 cells.
  • Utilized co-transfection, immunoprecipitation, FRET, and cAMP assays to study interactions and signaling.

Main Results:

  • Truncated β-subunits (β-316, -366) expressed on the cell surface, while β-409 was intracellular.
  • Co-expression with full-length TSHR significantly decreased its surface expression.
  • Confirmed dimerization between β-subunits and full-length TSHR.
  • TSHR signaling (cAMP generation) was reduced upon co-expression.
  • Faster internalization rates for truncated β-subunits were observed.

Conclusions:

  • Multimerization of cleaved TSHR β-subunits with full-length TSHR significantly impacts TSHR internalization and signaling.
  • This interaction leads to reduced cell surface expression and impaired TSH-induced cAMP generation.
  • The degree of TSHR intramolecular cleavage influences its signaling capacity.