Identification of a Preassembled TRH Receptor-Gq/11 Protein Complex in HEK293 Cells
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- Drastichova Zdenka
- Department of Physiology, Faculty of Science, Charles University
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- Novotny Jiri
- Department of Physiology, Faculty of Science, Charles University Institute of Physiology, Academy of Sciences of the Czech Republic
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Protein-protein interactions define specificity in signal transduction and these interactions are central to transmembrane signaling by G-protein-coupled receptors (GPCRs). It is not quite clear, however, whether GPCRs and the regulatory trimeric G-proteins behave as freely and independently diffusible molecules in the plasma membrane or whether they form some preassociated complexes. Here we used clear-native polyacrylamide gel electrophoresis (CN-PAGE) to investigate the presumed coupling between thyrotropin-releasing hormone (TRH) receptor and its cognate Gq/11 protein in HEK293 cells expressing high levels of these proteins. Under different solubilization conditions, the TRH receptor (TRH-R) was identified to form a putative pentameric complex composed of TRH-R homodimer and Gq/11 protein. The presumed association of TRH-R with Gq/11α or Gβ proteins in plasma membranes was verified by RNAi experiments. After 10- or 30-min hormone treatment, TRH-R signaling complexes gradually dissociated with a concomitant release of receptor homodimers. These observations support the model in which GPCRs can be coupled to trimeric G-proteins in preassembled signaling complexes, which might be dynamically regulated upon receptor activation. The precoupling of receptors with their cognate G-proteins can contribute to faster G-protein activation and subsequent signal transfer into the cell interior.<br>
収録刊行物
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- Cell Structure and Function
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Cell Structure and Function 37 (1), 1-12, 2012
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詳細情報 詳細情報について
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- CRID
- 1390001204696092032
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- NII論文ID
- 130004053884
- 40019581823
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- NII書誌ID
- AA0060007X
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- ISSN
- 13473700
- 03867196
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- NDL書誌ID
- 024271988
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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