Accessory proteins are vital for the functional expression of certain G protein-coupled receptors

Cooray, Sadani N.; Chan, Li F.; Webb, Tom R.; Metherell, Louise A.; Clark, Adrian

doi:10.1016/j.mce.2008.10.004

Cited by 35 publications

(19 citation statements)

References 53 publications

(50 reference statements)

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“…It is now well accepted that GPCRs can participate in noncanonical signaling networks via interactions with an expanding list of accessory proteins, often in a G protein-independent manner (Brady and Limbird, 2002;Sato et al, 2006;Cooray et al, 2009;Couvineau and Laburthe, 2012). Probably the best characterized example is that of the GPCR-b-arrestin interaction.…”

Section: Gpcr-accessory Protein Interactionsmentioning

confidence: 99%

Endogenous Allosteric Modulators of G Protein–Coupled Receptors

Westhuizen

Valant

Sexton

et al. 2015

J Pharmacol Exp Ther

132

131

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Section: Gpcr-accessory Protein Interactionsmentioning

confidence: 99%

Endogenous Allosteric Modulators of G Protein–Coupled Receptors

Westhuizen

Valant

Sexton

et al. 2015

J Pharmacol Exp Ther

132

131

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“…Current models postulate that animal receptor trafficking is controlled by ER membrane-localized receptor accessory proteins that bind to their cytoplasmic tails and recruit transport complexes (McLatchie et al, 1998;Petaja-Repo et al, 2000;Bermak et al, 2001;Dupré and Hé bert, 2006;Cooray et al, 2009;Díaz, 2010). Interestingly, RTNLB1 and RTNLB2 were also identified outside the ER compartment, namely, at the PM and in intracellular punctuate structures (Marmagne et al, 2004;Benschop et al, 2007;Nziengui et al, 2007;Mitra et al, 2009), suggesting their transport between various cellular compartments.…”

Section: Rtnlb1 and Rtnlb2 And Their Relationship With Two Processes mentioning

confidence: 99%

Arabidopsis RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

et al. 2011

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Receptors localized at the plasma membrane are critical for the recognition of pathogens. The molecular determinants that regulate receptor transport to the plasma membrane are poorly understood. In a screen for proteins that interact with the FLAGELIN-SENSITIVE2 (FLS2) receptor using Arabidopsis thaliana protein microarrays, we identified the reticulon-like protein RTNLB1. We showed that FLS2 interacts in vivo with both RTNLB1 and its homolog RTNLB2 and that a Ser-rich region in the N-terminal tail of RTNLB1 is critical for the interaction with FLS2. Transgenic plants that lack RTNLB1 and RTNLB2 (rtnlb1 rtnlb2) or overexpress RTNLB1 (RTNLB1ox) exhibit reduced activation of FLS2-dependent signaling and increased susceptibility to pathogens. In both rtnlb1 rtnlb2 and RTNLB1ox, FLS2 accumulation at the plasma membrane was significantly affected compared with the wild type. Transient overexpression of RTNLB1 led to FLS2 retention in the endoplasmic reticulum (ER) and affected FLS2 glycosylation but not FLS2 stability. Removal of the critical N-terminal Serrich region or either of the two Tyr-dependent sorting motifs from RTNLB1 causes partial reversion of the negative effects of excess RTNLB1 on FLS2 transport out of the ER and accumulation at the membrane. The results are consistent with a model whereby RTNLB1 and RTNLB2 regulate the transport of newly synthesized FLS2 to the plasma membrane.

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“…The overall structure of the Ost transporter, in which a larger multi-TM domain subunit is accompanied by a single TM accessory protein, occurs frequently in membrane proteins. Examples include certain G protein-coupled receptors, like Frizzled-LRP5/6, CRLR-RAMP1, and MC2R-MRAP (34,35); the nicotinic acetylcholine receptor, ␣7-nAchR-RIC-3 (36, 37); the K ϩ channel, K v 1.4-K v ␤3 (38, 39); the Na the larger subunit(s), (ii) escorting the larger subunit(s) to the plasma membrane, (iii) forming part of the active complex and assisting in its retention at the membrane, (iv) forming part of the ligand/substrate binding pocket, and (v) participating in desensitization and internalization.…”

Section: Discussionmentioning

confidence: 99%

“…Four residues are completely conserved: a Glu-Asp sequence (Glu 29 -Asp 30 ) near the N terminus of the TM helix, a Trp (Trp 34 ) at the predicted start of the TM domain, and an Arg (Arg 61 ) located eight amino acids from the C terminus of the TM domain. Also of note is the highly conserved Asn (Asn 35 ), which is present in all species except the zebrafish (Fig. 3A).…”

Section: Domains Of Ost␤ Required For Function-to Identify Regionsmentioning

confidence: 99%

β-Subunit of the Ostα-Ostβ Organic Solute Transporter Is Required Not Only for Heterodimerization and Trafficking but Also for Function

Christian

Hinkle

et al. 2012

Journal of Biological Chemistry

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Background: Deletion of Ost␣-Ost␤, an intestinal transporter that participates in the enterohepatic circulation of bile acids, lowers cholesterol and triglyceride levels. Results: Residues of Ost␤ required for interaction with Ost␣ and transport activity were identified. Conclusion: Distinct regions of Ost␤ are essential for Ost␣-Ost␤ trafficking and transport activity. Significance: Findings suggest strategies for inhibiting the holotransporter and reducing lipid levels.

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Accessory proteins are vital for the functional expression of certain G protein-coupled receptors

Cited by 35 publications

References 53 publications

Endogenous Allosteric Modulators of G Protein–Coupled Receptors

Endogenous Allosteric Modulators of G Protein–Coupled Receptors

Arabidopsis RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

β-Subunit of the Ostα-Ostβ Organic Solute Transporter Is Required Not Only for Heterodimerization and Trafficking but Also for Function

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