Molecular Identification and Characterization of G Protein-Coupled Receptors for Lysophosphatidic Acid and Sphingosine 1-Phosphate

2006 ◽  
Vol 905 (1) ◽  
pp. 25-33 ◽  
Author(s):  
SONGZHU AN
Keyword(s):  
G Protein ◽  
Molecular Identification ◽  
Lysophosphatidic Acid ◽  
G Protein Coupled Receptors ◽  
Sphingosine 1 Phosphate ◽  
G Protein Coupled ◽  
Identification And Characterization

scholarly journals Refolding and characterization of two G protein-coupled receptors purified from E. coli inclusion bodies

PLoS ONE ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. e0247689
Author(s):  
Bastian Heim ◽  
René Handrick ◽  
Marcus D. Hartmann ◽  
Hans Kiefer
Keyword(s):  
G Protein ◽  
Inclusion Bodies ◽  
Protein Unfolding ◽  
G Protein Coupled Receptors ◽  
Orphan Receptor ◽  
Cubic Phase ◽  
E Coli ◽  
Sphingosine 1 Phosphate ◽  
G Protein Coupled

Aiming at streamlining GPCR production from E. coli inclusion bodies for structural analysis, we present a generic approach to assess and optimize refolding yield through thermostability analysis. Since commonly used hydrophobic dyes cannot be applied as probes for membrane protein unfolding, we adapted a technique based on reacting cysteins exposed upon thermal denaturation with fluorescent 7-Diethylamino-3-(4-maleimidophenyl)-4-methylcoumarin (CPM). Successful expression, purification and refolding is shown for two G protein-coupled receptors (GPCR), the sphingosine-1-phosphate receptor S1P1, and the orphan receptor GPR3. Refolded receptors were subjected to lipidic cubic phase crystallization screening.

scholarly journals Identification and Characterization of Two G Protein-coupled Receptors for Neuropeptide FF

2000 ◽  
Vol 275 (50) ◽  
pp. 39324-39331 ◽  
Author(s):  
James A. Bonini ◽  
Kenneth A. Jones ◽  
Nika Adham ◽  
Carlos Forray ◽  
Roman Artymyshyn ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Coupled Receptors ◽  
Neuropeptide Ff ◽  
G Protein Coupled ◽  
Identification And Characterization

scholarly journals Current Knowledge on the Biology of Lysophosphatidylserine as an Emerging Bioactive Lipid

2021 ◽  
Author(s):  
Jumpei Omi ◽  
Kuniyuki Kano ◽  
Junken Aoki
Keyword(s):  
Immune System ◽  
Mast Cells ◽  
G Protein ◽  
Lysophosphatidic Acid ◽  
Immune Cells ◽  
Current Knowledge ◽  
G Protein Coupled Receptors ◽  
Sphingosine 1 Phosphate ◽  
Recent Developments ◽  
G Protein Coupled

AbstractLysophosphatidylserine (LysoPS) is an emerging lysophospholipid (LPL) mediator, which acts through G protein-coupled receptors, like lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P). LysoPS is detected in various tissues and cells and thought to be produced mainly by the deacylation of phosphatidylserine. LysoPS has been known to stimulate degranulation of mast cells. Recently, four LysoPS-specific G protein-coupled receptors (GPCRs) were identified. These GPCRs belong to the P2Y family which covers receptors for nucleotides and LPLs and are predominantly expressed in immune cells such as lymphocytes and macrophages. Studies on knockout mice of these GPCRs have revealed that LysoPS has immune-modulatory functions. Up-regulation of a LysoPS-producing enzyme, PS-specific phospholipase A1, was frequently observed in situations where the immune system is activated including autoimmune diseases and organ transplantations. Therefore, modulation of LysoPS signaling appears to be a promising method for providing therapies for the treatment of immune diseases. In this review, we summarize the biology of LysoPS-producing enzymes and receptors, recent developments in LysoPS signal modulators, and prospects for future therapeutic applications.

Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors

1996 ◽  
Vol 74 (4) ◽  
pp. 449-457 ◽  
Author(s):  
Jean-Pierre Morello ◽  
Michel Bouvier
Keyword(s):  
G Protein ◽  
Turnover Rate ◽  
G Protein Coupled Receptors ◽  
Regulatory Function ◽  
Post Translational Modification ◽  
Protein Membrane ◽  
G Protein Coupled ◽  
Identification And Characterization ◽  
Protein Acylation

Protein acylation is a post-translational modification that has seized much attention in the last few years. Depending on the nature of the fatty acid added, protein acylation can take the form of palmitoylation, myristoylation, or prenylation. Palmitoylation has been implicated in the modification of several different proteins and is particularly prevalent in G-protein coupled receptors and their cognate G-proteins, where it is thought to have an important regulatory function. Given that palmitoylation of these proteins is a dynamic phenomenon in which turnover rate is modulated by agonist activation, it is thought to be implicated in processes such as receptor phosphorylation and desensitization as well as in G-protein membrane translocation. A better understanding of the regulation of signal transduction mediated by G-protein coupled receptors will require the identification and characterization of those enzymes implicated in the palmitoylation and depalmitoylation process of this large class of receptors and their signalling allies.Key words: palmitoylation, β-adrenergic receptor, G-protein, phosphorylation, desensitization.

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