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Article: The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor

TitleThe truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor
Authors
KeywordsDominant-negative mutant
Ghrelin receptor
GHS-R1b
Issue Date2007
Citation
Cellular Signalling, 2007, v. 19, n. 5, p. 1011-1022 How to Cite?
AbstractThe dimerization properties of the ghrelin receptor (GRLN-R) and its non-signalling, naturally occurring, truncated splice variant (GHS-R1b) have been investigated in human embryonic kidney 293 cells heterologously expressing these proteins. Using the techniques of bioluminescence resonance energy transfer and co-immunoprecipitation, we detected the formation of GRLN-R homodimers and GRLN-R/GHS-R1b heterodimers, but ghrelin-induced conformational changes were only detected in the GRLN-R homodimers. When the expression of GHS-R1b exceeded that of GRLN-R, there was a decrease in the cell surface expression of GRLN-R with a consequent decrease in constitutive activation of phosphatidylinositol-specific phospholipase C (PI-PLC). Furthermore, there was no change in ghrelin affinity, and the efficacy of cell signalling as measured by stimulation of PI-PLC and extracellular signal-regulated kinase 1/2 was unchanged. Cellular localization studies suggest that GRLN-R is normally distributed between the plasma membrane and cytosolic fractions, but in the presence of GHS-R1b, GRLN-R is localized to the nucleus. Therefore, we propose that the decrease in GRLN-R constitutive signalling was due to translocation of GRLN-R to the nucleus due to the formation of GRLN-R/GHS-R1b heterodimers. Therefore, GHS-R1b appears to act as a dominant-negative mutant of the full-length GRLN-R. © 2006 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/225030
ISSN
2015 Impact Factor: 4.191
2015 SCImago Journal Rankings: 2.289

 

DC FieldValueLanguage
dc.contributor.authorLeung, Po Ki-
dc.contributor.authorChow, Kevin B S-
dc.contributor.authorLau, Pui Ngan-
dc.contributor.authorChu, Kit Man-
dc.contributor.authorChan, Chi Bun-
dc.contributor.authorCheng, Christopher H K-
dc.contributor.authorWise, Helen-
dc.date.accessioned2016-04-18T11:16:34Z-
dc.date.available2016-04-18T11:16:34Z-
dc.date.issued2007-
dc.identifier.citationCellular Signalling, 2007, v. 19, n. 5, p. 1011-1022-
dc.identifier.issn0898-6568-
dc.identifier.urihttp://hdl.handle.net/10722/225030-
dc.description.abstractThe dimerization properties of the ghrelin receptor (GRLN-R) and its non-signalling, naturally occurring, truncated splice variant (GHS-R1b) have been investigated in human embryonic kidney 293 cells heterologously expressing these proteins. Using the techniques of bioluminescence resonance energy transfer and co-immunoprecipitation, we detected the formation of GRLN-R homodimers and GRLN-R/GHS-R1b heterodimers, but ghrelin-induced conformational changes were only detected in the GRLN-R homodimers. When the expression of GHS-R1b exceeded that of GRLN-R, there was a decrease in the cell surface expression of GRLN-R with a consequent decrease in constitutive activation of phosphatidylinositol-specific phospholipase C (PI-PLC). Furthermore, there was no change in ghrelin affinity, and the efficacy of cell signalling as measured by stimulation of PI-PLC and extracellular signal-regulated kinase 1/2 was unchanged. Cellular localization studies suggest that GRLN-R is normally distributed between the plasma membrane and cytosolic fractions, but in the presence of GHS-R1b, GRLN-R is localized to the nucleus. Therefore, we propose that the decrease in GRLN-R constitutive signalling was due to translocation of GRLN-R to the nucleus due to the formation of GRLN-R/GHS-R1b heterodimers. Therefore, GHS-R1b appears to act as a dominant-negative mutant of the full-length GRLN-R. © 2006 Elsevier Inc. All rights reserved.-
dc.languageeng-
dc.relation.ispartofCellular Signalling-
dc.subjectDominant-negative mutant-
dc.subjectGhrelin receptor-
dc.subjectGHS-R1b-
dc.titleThe truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.cellsig.2006.11.011-
dc.identifier.pmid17229547-
dc.identifier.scopuseid_2-s2.0-33947301456-
dc.identifier.volume19-
dc.identifier.issue5-
dc.identifier.spage1011-
dc.identifier.epage1022-

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