Heterooligomerization of the D1 and D5 dopamine receptors.
Published: 2005
Language: eng
Number of pages: 101
Description: Many studies have demonstrated that G-protein coupled receptors (GPCRs) form dimeric and higher order oligomeric units both in-vivo and in-vitro. A study of the two closely related D1-like receptors D1 and D5, was performed in order to determine if an association existed. Using the co-immunoprecipitation as a starting point, we have established that D1 and D5 associate. We further explored this interaction through the use of a newly developed nuclear localization signal (NLS) based assay that displayed an interaction between the D1 and D5 dopamine receptors fused to fluorophores and expressed in HEK293T cells. Additionally, a cell-surface assay was performed, demonstrating that a NLS-inserted D1 or D5 receptor could effectively co-internalize with a non-NLS receptor, suggesting that an interaction between these two receptors existed. The NLS-based assay in combination with the previous data from the co-immunoprecipitation, demonstrated that the D1 and D5 dopamine receptors could form heterooligomers.
Notes: Source: Masters Abstracts International, Volume: 44-02, page: 0830.

Thesis (M.Sc.)--University of Toronto, 2005.

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