The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors.
The human leukocyte adhesion-G protein-coupled receptors (GPCRs), the epidermal growth factor (EGF)-TM7 proteins, are shown here to function as homo- and hetero-oligomers. Using cell surface cross-linking, co-immunoprecipitation, and fluorescence resonance energy transfer analysis of EMR2, an EGF-TM...
Main Authors: | , , , , , |
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Format: | Journal article |
Language: | English |
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2007
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author | Davies, J Chang, G Yona, S Gordon, S Stacey, M Lin, H |
author_facet | Davies, J Chang, G Yona, S Gordon, S Stacey, M Lin, H |
author_sort | Davies, J |
collection | OXFORD |
description | The human leukocyte adhesion-G protein-coupled receptors (GPCRs), the epidermal growth factor (EGF)-TM7 proteins, are shown here to function as homo- and hetero-oligomers. Using cell surface cross-linking, co-immunoprecipitation, and fluorescence resonance energy transfer analysis of EMR2, an EGF-TM7 receptor predominantly expressed in myeloid cells, we demonstrate that it forms dimers in a reaction mediated exclusively by the TM7 moiety. We have also identified a naturally occurring but structurally unstable EMR2 splice variant that acts as a dominant negative modulator by dimerizing with the wild type receptor and down-regulating its expression. Additionally, heterodimerization between closely related EGF-TM7 members is shown to result in the modulation of expression and ligand binding properties of the receptors. These findings suggest that receptor homo- and hetero-oligomerization play a regulatory role in modulating the expression and function of leukocyte adhesion-GPCRs. |
first_indexed | 2024-03-07T01:27:58Z |
format | Journal article |
id | oxford-uuid:929c8834-fc5c-42de-a3ec-9953aa0d18e0 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T01:27:58Z |
publishDate | 2007 |
record_format | dspace |
spelling | oxford-uuid:929c8834-fc5c-42de-a3ec-9953aa0d18e02022-03-26T23:26:44ZThe role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:929c8834-fc5c-42de-a3ec-9953aa0d18e0EnglishSymplectic Elements at Oxford2007Davies, JChang, GYona, SGordon, SStacey, MLin, HThe human leukocyte adhesion-G protein-coupled receptors (GPCRs), the epidermal growth factor (EGF)-TM7 proteins, are shown here to function as homo- and hetero-oligomers. Using cell surface cross-linking, co-immunoprecipitation, and fluorescence resonance energy transfer analysis of EMR2, an EGF-TM7 receptor predominantly expressed in myeloid cells, we demonstrate that it forms dimers in a reaction mediated exclusively by the TM7 moiety. We have also identified a naturally occurring but structurally unstable EMR2 splice variant that acts as a dominant negative modulator by dimerizing with the wild type receptor and down-regulating its expression. Additionally, heterodimerization between closely related EGF-TM7 members is shown to result in the modulation of expression and ligand binding properties of the receptors. These findings suggest that receptor homo- and hetero-oligomerization play a regulatory role in modulating the expression and function of leukocyte adhesion-GPCRs. |
spellingShingle | Davies, J Chang, G Yona, S Gordon, S Stacey, M Lin, H The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title | The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title_full | The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title_fullStr | The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title_full_unstemmed | The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title_short | The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. |
title_sort | role of receptor oligomerization in modulating the expression and function of leukocyte adhesion g protein coupled receptors |
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