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Phosphorylation of intracellular serine and threonine residues is the most important post translational modification of G protein-coupled receptors (GPCRs) also called heptahelical or seven transmembrane receptors (7TMR). After agonist exposure, these receptors acquire an active conformation, which is recognized by a family of highly specialized GPCR kinases (GRKs). Agonist-driven phosphorylation by GRKs regulates acute receptor desensitization, arrestin recruitment, internalization, post-activation signaling, long-term tolerance and drug addiction. Phosphosite-specific 7TM antibodies are designed to specifically detect agonist-activated GPCRs. In fact, recent work shows that ligand profiling using phosphosite-specific 7TM antibodies provides valuble information on ligand bias beyond that obtained with conventional ß-arrestin recruitment assays. Phosphosite-specific 7TM antibodies are novel tools for GPCR research that can be used to:

  • profile agonist properties of novel GPCR ligands
  • decipher the phosphorylation barcode of GPCRs
  • determine the spatial and temporal dynamics of receptor phosphorylation
  • identify relevant kinases and phosphatases for GPCR phosphorylation and dephosphoryation

Lifecycle3

Schematic representation of the G protein-coupled receptor phosphorylation / dephosphorylation cycle. GRK, G protein-coupled receptor kinase; PKC, protein kinase C; cPP1, catalytic subunit of protein phosphatase 1; R*, activated GPCR; CCP, clathrin-coated pit. 

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Agonist-induced Serine332/Serine333/Serine334 phosphorylation of the M3 Muscarinic Acetycholine Receptor.
pS332/pS333/pS334-M3 (phospho-M3 Muscarinic...
Serine332/Serine333/Serine334 is a major phosphorylation site of the M3 Muscarinic Acetylcholine Receptor. The pS332/pS333/pS334-M3 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation....
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Agonist-induced Serine315/Serine320 phosphorylation of the M2 Muscarinic Acetycholine Receptor
pS315/pS320-M2 (phospho-M2 Muscarinic...
Serine315/Serine320 is a major phosphorylation site of the M2 Muscarinic Acetylcholine Receptor. The pS315/pS320-M2 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. S315/S320...
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Agonist-induced Threonine310/Serine311 phosphorylation of the M2 Muscarinic Acetycholine Receptor
pT310/pS311-M2 (phospho-M2 Muscarinic...
Threonine310/Serine311 is a major phosphorylation site of the M2 Muscarinic Acetylcholine Receptor. The pT310/pS311-M2 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. T310/S311...
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Agonist-induced Serine286/Threonine287/Serine288 phosphorylation of the M2 Muscarinic Acetycholine Receptor
pS286/pT287/pS288-M2 (phospho-M2 Muscarinic...
Serine286/Threonine287/Serine288 is a major phosphorylation site of the M2 Muscarinic Acetylcholine Receptor. The pS286/pT287/pS288-M2 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation....
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Agonist-induced Serine298 phosphorylation of the M1 Muscarinic Acetylcholine Receptor
pS298-M1 (phospho-M1 Muscarinic Acetylcholine...
Serine298 is a major phosphorylation site of the M1 muscarinic acetylcholine receptor. The pS298-M1 antibody detects phosphorylation in response to high-efficacy agonists.
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Agonist-induced Threonine3545/Serine356 phosphorylation of the 5-Hydroxytryptamine Receptor 6
pT355/pS356-5-HT6 (phospho-5-HT Receptor 6...
Threonine355/Serine356 is a major phosphorylation site of the 5-HT6 receptor. The pT355/pS356-5-HT6 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. T355/S356 phosphorylation is a key...
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Agonist-induced Threonine370 phosphorylation of the Bombesin Receptor 3
pT370-BB3 (phospho-Bombesin Receptor 3 Antibody)
Threonine370 (T370) is major phosphorylation site of the Bombesin Receptor 3 (BB3). The pT370-BB3 antibody detects phosphorylation in response to agonists. T370 phosphorylation is likely to be involved in efficient ligand sequestration...
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Agonist-induced Threonine363/Threonine364 phosphorylation of the Bombesin Receptor 3
pT363/pT364-BB3 (phospho-Bombesin Receptor 3...
Threonine363/Threonine360 (T363/T364) is major phosphorylation site of the Bombesin Receptor 3 (BB3). The pT363/pT364-BB3 antibody detects phosphorylation in response to agonists. T363/T364 phosphorylation is likely to be involved in...
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Agonist-induced Threonine360/Serine361 phosphorylation of the Bombesin Receptor 3
pT360/pS361-BB3 (phospho-Bombesin Receptor 3...
Threonine360/Serine361 (T360/S361) is major phosphorylation site of the Bombesin Receptor 3 (BB3). The pT360/pS361-BB3 antibody detects phosphorylation in response to agonists. T360/S361 phosphorylation is likely to be involved in...
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Agonist-induced Threonine371 phosphorylation of the TRH1-Receptor
pT371-TRH1 (phospho-Thyrotropin-Releasing...
Threonine371 (T371) is a major phosphorylation site of the TRH1 receptor. The pT371-TRH1 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. T371 phosphorylation is primarily...
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Agonist-induced Serine364/Threonine365 phosphorylation of the TRH1-Receptor
pS364/pT365-TRH1 (phospho-Thyrotropin-Releasing...
Serine364/Threonine365 (S364/T365) is a major phosphorylation site of the TRH1 receptor. The pS364/pT365-TRH1 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S364/T365...
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Agonist-induced Serine360 phosphorylation of the TRH1-Receptor
pS360-TRH1 (phospho-Thyrotropin-Releasing...
Serine360 (S360) is a major phosphorylation site of the TRH1 receptor. The pS360-TRH1 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S360 phosphorylation is primarily...
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Agonist-induce Serine364/Serine366 phosphorylation of the EP4 Prostanoid Receptor
pS364/pS366-EP4 (phospho-EP4 Prostanoid...
Serine364/Serine366 (S364/S366) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pS364/pS366-EP4 antibody detects phosphorylation in response to agonists. S364/S366 phosphorylation is likely to be involved in...
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Agonist-induced Serine374/Serine377 phosphorylation of the EP4 Prostanoid Receptor
pS374/pS377-EP4 (phospho-EP4 Prostanoid...
Serine374/Serine377 (S374/S377) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pS374/pS377-EP4 antibody detects phosphorylation in response to agonists. S374/S377 phosphorylation is likely to be involved in...
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pT369/pS370-EP4 (phospho-EP4 Prostanoid Receptor Antibody)
pT369/pS370-EP4 (phospho-EP4 Prostanoid...
Threonine369/Serine370 (T369/S370) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pT369/pS370-EP4 antibody detects phosphorylation in response to agonists. T369/S370 phosphorylation is likely to be involved in...
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Agonist-induced Serine347/Threonine348phosphorylation of the EP2 Prostanoid Receptor
pS347/pT348-EP2 (phospho-EP2 Prostanoid...
Serine347/Threonine348 (S347/T348) is major phosphorylation site of the EP2 Prostanoid Receptor (EP2). The pS347/pT348-EP2 antibody detects phosphorylation in response to agonists. S347/T348 phosphorylation is likely to be involved in...
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17 From 37

For further reading refer to:

Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636. doi:10.1016/j.tips.2017.04.002. Epub 2017 May 4. Review. PubMed PMID: 28478994.

Miess E, Gondin AB, Yousuf A, Steinborn R, Mösslein N, Yang Y, Göldner M, Ruland JG, Bünemann M, Krasel C, Christie MJ, Halls ML, Schulz S, Canals M. Multisite phosphorylation is required for sustained interaction with GRKs and arrestins during rapid μ-opioid receptor desensitization. Sci Signal. 2018 Jul 17;11(539). pii: eaas9609. doi: 10.1126/scisignal.aas9609. PubMed PMID: 30018083.

Kliewer A, Schmiedel F, Sianati S, Bailey A, Bateman JT, Levitt ES, Williams JT, Christie MJ, Schulz S. Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects. Nat Commun. 2019 Jan 21;10(1):367. doi: 10.1038/s41467-018-08162-1. PubMed PMID: 30664663; PubMed Central PMCID: PMC6341117.

Mann A, Moulédous L, Froment C, O'Neill PR, Dasgupta P, Günther T, Brunori G, Kieffer BL, Toll L, Bruchas MR, Zaveri NT, Schulz S. Agonist-selective NOP receptor phosphorylation correlates in vitro and in vivo and reveals differential post-activation signaling by chemically diverse agonists. Sci Signal. 2019 Mar 26;12(574). pii: eaau8072. doi: 10.1126/scisignal.aau8072. PubMed PMID: 30914485; PubMed Central PMCID: PMC6934085.

Saaber F, Schütz D, Miess E, Abe P, Desikan S, Ashok Kumar P, Balk S, Huang K, Beaulieu JM, Schulz S, Stumm R. ACKR3 Regulation of Neuronal Migration Requires ACKR3 Phosphorylation, but Not β-Arrestin. Cell Rep. 2019 Feb 5;26(6):1473-1488.e9. doi: 10.1016/j.celrep.2019.01.049. PubMed PMID: 30726732.

Glück L, Loktev A, Moulédous L, Mollereau C, Law PY, Schulz S. Loss of morphine reward and dependence in mice lacking G protein-coupled receptor kinase 5. Biol Psychiatry. 2014 Nov 15;76(10):767-74. doi: 10.1016/j.biopsych.2014.01.021. Epub 2014 Feb 3. PubMed PMID: 24629717; PubMed Central PMCID: PMC4119866.

For further reading refer to: Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636.... read more »
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For further reading refer to:

Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636. doi:10.1016/j.tips.2017.04.002. Epub 2017 May 4. Review. PubMed PMID: 28478994.

Miess E, Gondin AB, Yousuf A, Steinborn R, Mösslein N, Yang Y, Göldner M, Ruland JG, Bünemann M, Krasel C, Christie MJ, Halls ML, Schulz S, Canals M. Multisite phosphorylation is required for sustained interaction with GRKs and arrestins during rapid μ-opioid receptor desensitization. Sci Signal. 2018 Jul 17;11(539). pii: eaas9609. doi: 10.1126/scisignal.aas9609. PubMed PMID: 30018083.

Kliewer A, Schmiedel F, Sianati S, Bailey A, Bateman JT, Levitt ES, Williams JT, Christie MJ, Schulz S. Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects. Nat Commun. 2019 Jan 21;10(1):367. doi: 10.1038/s41467-018-08162-1. PubMed PMID: 30664663; PubMed Central PMCID: PMC6341117.

Mann A, Moulédous L, Froment C, O'Neill PR, Dasgupta P, Günther T, Brunori G, Kieffer BL, Toll L, Bruchas MR, Zaveri NT, Schulz S. Agonist-selective NOP receptor phosphorylation correlates in vitro and in vivo and reveals differential post-activation signaling by chemically diverse agonists. Sci Signal. 2019 Mar 26;12(574). pii: eaau8072. doi: 10.1126/scisignal.aau8072. PubMed PMID: 30914485; PubMed Central PMCID: PMC6934085.

Saaber F, Schütz D, Miess E, Abe P, Desikan S, Ashok Kumar P, Balk S, Huang K, Beaulieu JM, Schulz S, Stumm R. ACKR3 Regulation of Neuronal Migration Requires ACKR3 Phosphorylation, but Not β-Arrestin. Cell Rep. 2019 Feb 5;26(6):1473-1488.e9. doi: 10.1016/j.celrep.2019.01.049. PubMed PMID: 30726732.

Glück L, Loktev A, Moulédous L, Mollereau C, Law PY, Schulz S. Loss of morphine reward and dependence in mice lacking G protein-coupled receptor kinase 5. Biol Psychiatry. 2014 Nov 15;76(10):767-74. doi: 10.1016/j.biopsych.2014.01.021. Epub 2014 Feb 3. PubMed PMID: 24629717; PubMed Central PMCID: PMC4119866.

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