Homo- and hetero-dimerization of LPA/S1P receptors, OGR1 and GPR4

Alexander Zaslavsky, Lisam Shanjukumar Singh, Haiyan Tan, Huawen Ding, Zicai Liang, Yan Xu

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

G protein coupled receptors (GPCRs) form homo- and hetero-dimers or -oligomers, which are functionally important. Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are bioactive lysophopholipids involved in diverse biological processes. We have examined homo- and hetero-dimerization among three major LPA receptors (LPA1-3), three major S1P receptors (S1P1-3), as well as OGR1 and GPR4. Using LacZ complementation assays, we have shown that LPA receptors form homo- and hetero-dimers within the LPA receptor subgroup and hetero-dimers with other receptors (S1P1-3 and GPR4). In addition, we have found that although GPR4 and OGR1 share more than 50% homology, GPR4 forms strong homo- and hetero-dimers with LPA and S1P receptors, but OGR1 forms very weak homo-dimer and relatively weak hetero-dimers with other receptors. Using chimeric receptors between GPR4 and OGR1, we have shown that different domains of GPR4 receptor are involved in its dimerization with different GPCRs and more than one domain may be involved in some of the complex formation. Our results suggest that when studying a signal transduction induced by a stimulus, not only is the expression and activation of its own receptor(s), but also the status of the interacting receptors should be taken into consideration.

Original languageEnglish
Pages (from-to)1200-1212
Number of pages13
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume1761
Issue number10
DOIs
StatePublished - Oct 2006

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Lysophosphatidic Acid Receptors
Lysosphingolipid Receptors
Hominidae
Dimerization
G-Protein-Coupled Receptors
Biological Phenomena
Signal Transduction
lysophosphatidic acid

Keywords

  • β-galactosidase (LacZ)
  • G protein couple receptors (GPCRs)
  • LPA receptors (LPA, LPA and LPA)
  • Lysophosphatidic acid (LPA)
  • OGR1 and GPR4
  • S1P receptors (S1P, S1P, and S1P)
  • Sphingosine-1-phosphate (S1P)

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biophysics

Cite this

Homo- and hetero-dimerization of LPA/S1P receptors, OGR1 and GPR4. / Zaslavsky, Alexander; Singh, Lisam Shanjukumar; Tan, Haiyan; Ding, Huawen; Liang, Zicai; Xu, Yan.

In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, Vol. 1761, No. 10, 10.2006, p. 1200-1212.

Research output: Contribution to journalArticle

Zaslavsky, Alexander ; Singh, Lisam Shanjukumar ; Tan, Haiyan ; Ding, Huawen ; Liang, Zicai ; Xu, Yan. / Homo- and hetero-dimerization of LPA/S1P receptors, OGR1 and GPR4. In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids. 2006 ; Vol. 1761, No. 10. pp. 1200-1212.
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abstract = "G protein coupled receptors (GPCRs) form homo- and hetero-dimers or -oligomers, which are functionally important. Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are bioactive lysophopholipids involved in diverse biological processes. We have examined homo- and hetero-dimerization among three major LPA receptors (LPA1-3), three major S1P receptors (S1P1-3), as well as OGR1 and GPR4. Using LacZ complementation assays, we have shown that LPA receptors form homo- and hetero-dimers within the LPA receptor subgroup and hetero-dimers with other receptors (S1P1-3 and GPR4). In addition, we have found that although GPR4 and OGR1 share more than 50{\%} homology, GPR4 forms strong homo- and hetero-dimers with LPA and S1P receptors, but OGR1 forms very weak homo-dimer and relatively weak hetero-dimers with other receptors. Using chimeric receptors between GPR4 and OGR1, we have shown that different domains of GPR4 receptor are involved in its dimerization with different GPCRs and more than one domain may be involved in some of the complex formation. Our results suggest that when studying a signal transduction induced by a stimulus, not only is the expression and activation of its own receptor(s), but also the status of the interacting receptors should be taken into consideration.",
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AU - Zaslavsky, Alexander

AU - Singh, Lisam Shanjukumar

AU - Tan, Haiyan

AU - Ding, Huawen

AU - Liang, Zicai

AU - Xu, Yan

PY - 2006/10

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N2 - G protein coupled receptors (GPCRs) form homo- and hetero-dimers or -oligomers, which are functionally important. Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are bioactive lysophopholipids involved in diverse biological processes. We have examined homo- and hetero-dimerization among three major LPA receptors (LPA1-3), three major S1P receptors (S1P1-3), as well as OGR1 and GPR4. Using LacZ complementation assays, we have shown that LPA receptors form homo- and hetero-dimers within the LPA receptor subgroup and hetero-dimers with other receptors (S1P1-3 and GPR4). In addition, we have found that although GPR4 and OGR1 share more than 50% homology, GPR4 forms strong homo- and hetero-dimers with LPA and S1P receptors, but OGR1 forms very weak homo-dimer and relatively weak hetero-dimers with other receptors. Using chimeric receptors between GPR4 and OGR1, we have shown that different domains of GPR4 receptor are involved in its dimerization with different GPCRs and more than one domain may be involved in some of the complex formation. Our results suggest that when studying a signal transduction induced by a stimulus, not only is the expression and activation of its own receptor(s), but also the status of the interacting receptors should be taken into consideration.

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