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- Publisher Website: 10.1016/j.cellsig.2006.11.011
- Scopus: eid_2-s2.0-33947301456
- PMID: 17229547
- WOS: WOS:000245736200013
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Article: The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor
Title | The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor |
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Authors | |
Keywords | Dominant-negative mutant Ghrelin receptor GHS-R1b |
Issue Date | 2007 |
Citation | Cellular Signalling, 2007, v. 19, n. 5, p. 1011-1022 How to Cite? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/225030 |
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 1.317 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Leung, Po Ki | - |
dc.contributor.author | Chow, Kevin B S | - |
dc.contributor.author | Lau, Pui Ngan | - |
dc.contributor.author | Chu, Kit Man | - |
dc.contributor.author | Chan, Chi Bun | - |
dc.contributor.author | Cheng, Christopher H K | - |
dc.contributor.author | Wise, Helen | - |
dc.date.accessioned | 2016-04-18T11:16:34Z | - |
dc.date.available | 2016-04-18T11:16:34Z | - |
dc.date.issued | 2007 | - |
dc.identifier.citation | Cellular Signalling, 2007, v. 19, n. 5, p. 1011-1022 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.uri | http://hdl.handle.net/10722/225030 | - |
dc.description.abstract | The 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.language | eng | - |
dc.relation.ispartof | Cellular Signalling | - |
dc.subject | Dominant-negative mutant | - |
dc.subject | Ghrelin receptor | - |
dc.subject | GHS-R1b | - |
dc.title | The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.cellsig.2006.11.011 | - |
dc.identifier.pmid | 17229547 | - |
dc.identifier.scopus | eid_2-s2.0-33947301456 | - |
dc.identifier.volume | 19 | - |
dc.identifier.issue | 5 | - |
dc.identifier.spage | 1011 | - |
dc.identifier.epage | 1022 | - |
dc.identifier.isi | WOS:000245736200013 | - |
dc.identifier.issnl | 0898-6568 | - |