Assembly-dependent Surface Targeting of the Heterodimeric GABAB Receptor Is Controlled by COPI but Not 14-3-3
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Cell surface expression of transmembrane proteins is strictly regulated. Mutually exclusive interaction with COPI or 14-3-3 proteins has been proposed as a mechanism underlying such trafficking control of various proteins. In particular, 14-3-3 dimers have been proposed to "sense" correctly assembled oligomers, allowing their surface targeting by preventing COPI-mediated intracellular retention. Here we examined whether such a mechanism is involved in the quality control of the heterodimeric G protein-coupled GABAB receptor. Its GB1 subunit, carrying the retention signal RSR, only reaches the cell surface when associated with the GB2 subunit. We show that COPI and 14-3-3 specifically bind to the GB1 RSR sequence and that COPI is involved in its intracellular retention. However, we demonstrate that the interaction with 14-3-3 is not required for proper function of the GABAB receptor quality control. Accordingly, competition between 14-3-3 and COPI cannot be considered as a general trafficking control mechanism. A possible other role for competition between COPI and 14-3-3 binding is discussed.
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RRQR motifs are thought to prevent the exit of cargo from the ER and may additionally function as ER retrieval motifs via the binding of the RRXR domain to COPI proteins.
“RRQR motifs are thought to prevent the exit of cargo from the ER and may additionally function as ER retrieval motifs via the binding of the RRXR domain to COPI proteins (Scott et al., 2001, 2003; Brock et al., 2005; Michelsen et al., 2005).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Brock et al., 2005
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- Villemure, J.-F., Adam, L., Bevan, N. J., Gearing, K., Chénier, S., and Bouvier, M. (2005). Sub-cellular distribution of GABAB receptor homo- and heterodimers. Biochem. J. 388, 47–55. [DOI] [PMC free article] [PubMed] [Google Scholar]
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Self-citationCalmodulin Is a 5-HT Receptor-Interacting and Regulatory Protein
Chattopadhyay, A. (2007) · CRC Press eBooks · doi:10.1201/9781420005752-9 · Cited by 4 · see citing works
Time-resolved FRET approaches to study GPCR complexes
Pin, J., Maurel, D., Comps‐Agrar, L., Monnier, C., Rives, M., Doumazane, E., Rondard, P., Durroux, T., Prézeau, L., & Trinquet, E. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511760334.005 · Cited by 4 · see citing works
Self-citationMolecular Organization, Trafficking, and Degradation of the GABAB Receptor
Benke, D., Balakrishnan, K. R., & Zemoura, K. (2016) · Springer eBooks · doi:10.1007/978-3-319-46044-4_4 · Cited by 4 · see citing works
The localization of the ER retrieval sequence for the calcium pump SERCA1
Watson, H., Butler, J., Schuppe, H., LEE, A. G. J., & East, J. M. (2011) · Molecular Membrane Biology · doi:10.3109/09687688.2011.572566 · Cited by 4 · see citing works
A privileged ER compartment for posttranslational heteromeric assembly of an ion channel
Kannan, S., Kasberg, W., Ernandez, L. R., Audhya, A., & Robertson, G. A. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2500218122 · Cited by 3 · see citing works
Selective Cell-Surface Expression of Triheteromeric NMDA Receptors
Yi, F., Traynelis, S. F., & Hansen, K. B. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3830-9_5 · Cited by 3 · see citing works
Récepteurs GABABet sensibilisation douloureuse
Landry, M., & Nagy, F. (2009) · Journal de la Société de Biologie · doi:10.1051/jbio:2009009 · Cited by 3 · see citing works
Dimeric GPCRs: what did we learn from the metabotropic glutamate receptors?
Pin, J., Goudet, C., Kniazeff, J., Hlaváčková, V., Brock, C., Binet, V., Maurel, D., Rondard, P., Blahoš, J., & Prézeau, L. (2006) · Springer eBooks · doi:10.1007/3-540-34447-0_7 · Cited by 3 · see citing works
Self-citationThe intracellular C-terminal domain of mGluR6 contains ER retention motifs
Shimohata, A., Rai, D., Akagi, T., Usui, S., Ogiwara, I., & Kaneda, M. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103875 · Cited by 2 · see citing works
The Unusual Functioning of the GABAB-Receptor Heterodimer
Couve, A., Moss, S. J., & Pangalos, M. N. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-465-0_10 · Cited by 2 · see citing works
Benke, D., Bhat, M. A., & Hleihil, M. (2024) · The Receptors · doi:10.1007/978-3-031-67148-7_1 · Cited by 2 · see citing works
Small G Proteins: Arf Family GTPases in Vesicular Transport
Adolf, F., & Wieland, F. (2014) · Springer eBooks · doi:10.1007/978-3-319-07761-1_9 · Cited by 2 · see citing works
Calmodulin Is a 5-HT Receptor-Interacting and Regulatory Protein
Coaxum, S. D., Garnovskaya, M. N., Raymond, J. R., Turner, J. H., & Gelasco, A. K. (2007) · Frontiers in neuroscience · doi:10.1201/9781420005752.ch4 · Cited by 2 · see citing works
- Authors
- Brock, C., Boudier, L., Maurel, D., Blahos, J., & Pin, J.-P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- CNRS UMR5203, Montpellier F-34094 France
- Venue
- Molecular Biology of the Cell
- Published
- 2005-12
- Volume
- 16
- Issue
- 12
- Pages
- 5572-5578
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC1289403
- OpenAlex
- W2147149270
- Cited by
- 81
- References
- 30
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 5 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 5 · 2014: 8 · 2013: 2 · 2012: 6
- FWCI
- 3.53
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Keywords
- GABAB receptors, COPI, 14-3-3 proteins, cell surface targeting, intracellular retention, protein assembly, protein trafficking
- MeSH terms
- Biological Transport, Cell Line, Cell Membrane, Cloning, Molecular, Humans, Kidney, Kinetics, Transfection, Polymerase Chain Reaction, Receptors, GABA-B, Microscopy, Confocal, Dimerization, Coat Protein Complex I, 14-3-3 Proteins
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