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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 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-induced Serine369/Serine374 phosphorylation of the Neuropeptide Y receptor 2
pS369/pS374-NPY2 (phospho-Neuropeptide Y...
Serine369/Serine374 (S369/S374) is a major phosphorylation site of the Neuropeptide Y Receptor 2. The pS369/pS374-NPY2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation....
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Agonist-induced Serine354/Threonine356 phosphorylation of the Neuropeptide Y receptor 2
pS354/pT356-NPY2 (phospho-Neuropeptide Y...
Serine354Threonine356 (S354/T356) is a major phosphorylation site of the Neuropeptide Y Receptor 2. The pS354/pT356-NPY2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation....
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Agonist-induced Serine351/Serine354 phosphorylation of the Neuropeptide Y
pS351/pS354-NPY2 (phospho-Neuropeptide Y...
Serine351/Serine354 (S351/S354) is a major phosphorylation site of the Neuropeptide Y Receptor 2. The pS351/pS354-NPY2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation....
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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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Agonist-induced Threonine337/Serine340 phosphorylation of the TP Thromboxane Receptor
pT337/pS340-TP (phospho-TP Thromboxane Receptor...
Threonine337/Serine340 (T337/S340) is major phosphorylation site of the TP Thromboxane Receptor (TP). The pT337/pS340-TP antibody detects phosphorylation in response to agonists. T337/S340 phosphorylation is likely to be involved in...
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Agonist-induced Serine324/Serine328 phosphorylation of the IP Prostacyclin Receptor
pS324/pS328-IP (phospho-IP Prostacyclin...
Serine324/Serine328 (S324/S328) is major phosphorylation site of the IP Prostacyclin Receptor (IP). The pS324/pS328-IP antibody detects phosphorylation in response to agonists. S324/S328 phosphorylation is likely to be involved in...
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Agonist-induced Serine319/Threonine321 phosphorylation of the IP Prostacyclin Receptor
pS319/pT321-IP (phospho-IP Prostacyclin...
Serine319/Threonine321 (S319/T321) is major phosphorylation site of the IP Prostacyclin Receptor (IP). The pS319/pT321-IP antibody detects phosphorylation in response to agonists. S319/T321 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 Serine379/Serine380 phosphorylation of the EP3 Prostanoid Receptor
pS379/pS380-EP3 (phospho-EP3 Prostanoid...
Serine379/Serine380 (S379/S380) is major phosphorylation site of the EP3 Prostanoid Receptor (EP3). The pS379/pS380-EP3 antibody detects phosphorylation in response to agonists. S379/S380 phosphorylation is likely to be involved in...
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Agonist-induced Threonine372/Serine373 phosphorylation of the EP3 Prostanoid Receptor
pT372/pS373-EP3 (phospho-EP3 Prostanoid...
Threonine372/Serine373 (T372/S373) is major phosphorylation site of the EP3 Prostanoid Receptor (EP3). The pT372/pS373-EP3 antibody detects phosphorylation in response to agonists. T372/S373 phosphorylation is likely to be involved in...
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Agonist-induced Serine369/Serine370 phosphorylation of the EP3 Prostanoid Receptor
pS369/pS370-EP3 (phospho-EP3 Prostanoid...
Serine369/Serine370 (S369/S370) is major phosphorylation site of the EP3 Prostanoid Receptor (EP3). The pS369/pS370-EP3 antibody detects phosphorylation in response to agonists. S369/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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Agonist-induced Threonine344/Serine345 phosphorylation of the EP2 Prostanoid Receptor
pT344/pS345-EP2 (phospho-EP2 Prostanoid...
Threonine344/Serine345 (T344/S345) is major phosphorylation site of the EP2 Prostanoid Receptor (EP2). The pT344/pS345-EP2 antibody detects phosphorylation in response to agonists. T344/S345 phosphorylation is likely to be involved in...
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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.

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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