Abstract
In this thesis I demonstrate how the natural compositional heterogeneities of synthetic and
living cell model systems can be used to quantitate the mechanics of G-protein coupled
receptor (GPCR) oligomerization with Förster resonance energy transfer (FRET). The
thesis is structured around three appended manuscripts that investigate 1) the intrinsic
nature of GPCR oligomerization in the simple lipid environment of a proteoliposome, 2) the
regulation of GPCR oligomerization by membrane curvature, and 3) the extent of
heterogeneities in GPCR oligomerization within the plasma membrane of living cells and
the consequences of single cell and ensemble cell population averaging. I report new
findings that contribute to the collective understanding of GPCR oligomerization and
present methods easily amendable to investigate a wide range of protein – protein
interactions.
living cell model systems can be used to quantitate the mechanics of G-protein coupled
receptor (GPCR) oligomerization with Förster resonance energy transfer (FRET). The
thesis is structured around three appended manuscripts that investigate 1) the intrinsic
nature of GPCR oligomerization in the simple lipid environment of a proteoliposome, 2) the
regulation of GPCR oligomerization by membrane curvature, and 3) the extent of
heterogeneities in GPCR oligomerization within the plasma membrane of living cells and
the consequences of single cell and ensemble cell population averaging. I report new
findings that contribute to the collective understanding of GPCR oligomerization and
present methods easily amendable to investigate a wide range of protein – protein
interactions.
| Original language | English |
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| Publisher | Department of Chemistry, Faculty of Science, University of Copenhagen |
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| Number of pages | 125 |
| Publication status | Published - 2016 |