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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 Threonine377 phosphorylation of GPR88-Receptor
pT377-GPR88 (phospho-GPR88 Antibody)
Threonine377 (T377) is a major phosphorylation site of the human GPR88 receptor. The pT377-GPR88 antibody detects phosphorylation in response to high-efficacy agonists. T377 phosphorylation is a key regulator of human GPR88...
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NEW
Agonist-induced Serine346/Serine349 phosphorylation of GPR88-Receptor
pS346/pS349-GPR88 (phospho-GPR88 Antibody)
Serine346/Serine349 (S346/S349) is a major phosphorylation site of the human GPR88 receptor. The pS346/pS349-GPR88 antibody detects phosphorylation in response to high-efficacy agonists. S346/S349 phosphorylation is a key regulator of...
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NEW
Agonist-induced Serine371 phosphorylation of GPR88-Receptor.
pS371-GPR88 (phospho-GPR88 Antibody)
Serine371 (S371) is a major phosphorylation site of the human GPR88 receptor. The pS371-GPR88 antibody detects phosphorylation in response to high-efficacy agonists. S371 phosphorylation is a key regulator of human GPR88 desensitization,...
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NEW
Agonist-induced Threonine365/Serine371/Threonine377 phosphorylation of GPR88-Receptor
pT365/pS371/pT377-GPR88 (phospho-GPR88 Antibody)
Threonine365/Serine371/Threonine377 (T365/S371/T377) is a major phosphorylation site of the human GPR88 receptor. The pT365/pS371/pT377-GPR88 antibody detects phosphorylation in response to high-efficacy agonists. T365/S371/T377...
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NEW
Validation of the G Protein-coupled Receptor 17 in transfected HEK293 cells
GPR17 (GP-non-phospho), G Protein-coupled...
The non-phospho-GPR17 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human GPR17. It can be used to detect total GPR17 receptors in Western blots independent of phosphorylation. The...
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NEW
Validation of the Angiotensin Receptor 1 in transfected HEK293 cells
AT1 (GP-non-phospho) Angiotensin Receptor 1...
The non-phospho-AT1 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human Angiotensin Receptor 1 (AT1). It can be used to detect total AT1 receptors in Western blots independent of phosphorylation....
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NEW
Validation of the BLT1 Receptor in transfected HEK293 cells.
BLT1 (non-phospho), Leukotriene Receptor BLT1...
The non-phospho-BLT1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human BLT1. It can be used to detect total BLT1 receptors in Western blots independent of phosphorylation. The BLT1 antibody can...
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NEW
Validation of the GPR37 Receptor in transfected HEK293 cells
GPR37 (non-phospho), G protein-coupled Receptor...
The non-phospho-GPR37 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR37. It can be used to detect total GPR37 receptors in Western blots independent of phosphorylation. The GPR37 antibody...
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NEW
Validation of the GPR45 Receptor in transfected HEK293 cells.
GPR45 (non-phospho), G protein-coupled Receptor...
The non-phospho-GPR45 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR45. It can be used to detect total GPR45 receptors in Western blots independent of phosphorylation. The GPR45 antibody...
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NEW
Validation of the GPR135 Receptor in transfected HEK293 cells.
GPR135 (non-phospho), G protein-coupled...
The non-phospho-GPR135 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR135. It can be used to detect total GPR135 receptors in Western blots independent of phosphorylation. The GPR135...
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NEW
Validation of the GPR142 Receptor in transfected HEK293 cells.
GPR142 (non-phospho), G protein-coupled...
The non-phospho-GPR142 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR142. It can be used to detect total GPR142 receptors in Western blots independent of phosphorylation. The GPR142...
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NEW
Validation of the Lysophosphatidic Acid Receptor 6 in transfected HEK293 cells.
LPA6 (non-phospho), Lysophosphatidic Acid...
The non-phospho-LPA6 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human LPA6. It can be used to detect total LPA6 receptors in Western blots independent of phosphorylation. The LPA6 antibody can...
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NEW
Validation of the Lysophosphatidic Acid Receptor 4 in transfected HEK293 cells.
LPA4 (non-phospho), Lysophosphatidic Acid...
The non-phospho-LPA4 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human LPA4. It can be used to detect total LPA4 receptors in Western blots independent of phosphorylation. The LPA4 antibody can...
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NEW
Validation of the Lysophosphatidic Acid Receptor 1 in transfected HEK293 cells.
LPA1 (GP-non-phospho), Lysophosphatidic Acid...
The non-phospho-LPA1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human LPA1. It can be used to detect total LPA1 receptors in Western blots independent of phosphorylation. The LPA1 antibody can...
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NEW
Validation of the GPR161 Receptor in transfected HEK293 cells
GPR161 (GP-non-phospho), G protein-coupled...
The non-phospho-GPR161 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR161. It can be used to detect total GPR161 receptors in Western blots independent of phosphorylation. The GPR161...
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Citations
Validation of the Parathyroid Hormone Receptor 1 in transfected HEK293 cells
PTH1 (GP-non-phospho-Parathyroid Hormone...
The PTH1 antibody is directed against the distal end of the carboxyl-terminal tail of human Parathyroid Hormone Receptor 1. It can be used to detect total PTH1 receptors in Western blots independent of phosphorylation. The PTH1 antibody...
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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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