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Τίτλος – Title
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Νέα Σηματοδοτικά Μονοπάτια που Επάγονται από την Ενεργοποίηση του δ-Οπιοειδούς Υποδοχέα New Signaling Pathways Induced by Activation of δ-Opioid Receptor |
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Συγγραφέας – Author
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Ειρήνη-Μαρία Γεωργαντά, Αδαμαντία Αγάλου, Ζαφειρούλα Γεωργούση Εργαστήριο Κυταρικής Σηματοδότησης και Μοριακής Φαρμακολογίας, Ινστιτούτο Βιολογίας, Εθνικό Κέντρο Έρευνας Φυσικών Επιστημών Δημόκριτος, Αγία Παρασκευή Αττικκής Eirine-Maria Georganta, Adamantia Agalou, Zafeiroula Georgoussi Laboratory of Cellular Signaling and Molecular Pharmacology, Institute of Biology, National Center for Scientific Research Demokritos, Ag, Paraskevi 15310, Athens, Hellas |
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Παραπομπή – Citation
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Γεωργαντά,Ε.-Μ., Αγάλου,Α., Γεωργούση,Ζ. : Νέα Σηματοδοτικά Μονοπάτια που Επάγονται από την Ενεργοποίηση του δ-Οπιοειδούς Υποδοχέα, Επιθεώρηση Κλιν. Φαρμακολ. Φαρμακοκινητ. 27: 16-18 (2009)
Georganta,E.-M., Agalou,A., Georgoussi,Z. : New Signaling Pathways Induced by Activation of δ-Opioid Receptor, Epitheorese Klin. Farmakol. Farmakokinet. 27: 16-18 (2009)
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Ημερομηνία Δημοσιευσης – Publication Date
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8 Μαρτίου 2009 – 2009-03-08
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Γλώσσα Πλήρους Κειμένου –
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Ελληνικά – Greek |
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Λέξεις κλειδιά – Keywords
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δ-Οπιοειδής υποδοχέας, STAT5B μεταγραφικός παράγοντας, σηματοδοτικό σύμπλοκο, φωσφορυλίωση
δ-Opioid receptor, STAT5B transcriptional factor, signaling complex, phosphorylation
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Λοιποί Όροι – Other Terms
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Άρθρο Article |
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Περίληψη – Summary
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– The C-terminal domain of the δ-opioid receptor (δ-OR) consists of 62 amino acids and contains the consensus 317YAFL320 motif. Recent observations from our laboratory have shown that the conserved YXXL motif within the C-terminal tail of μ-opioid receptor (μ-OR) serves as a docking site for STAT5A transcriptional factor binding with the latter being phosphorylated upon μ-OR stimulation (4). In this regard, we sought to determine whether members of the STAT5 transcriptional factors interact also with the δ-OR and whether STAT5 phosphorylation is a universal signaling pathway among the opioid receptors. Coimmunoprecipitation and pull-down assays, using a GST fusion peptide encompassing the C-terminal region of the δ-OR (δ-CT), have shown that STAT5Β interacts directly with δ-OR. A truncated version of the δ-CT that lacks the first 26 amino acids indicated the importance of the N-terminal portion of the δ-CT for STAT5B binding. Additional co-immunoprecipitation experiments showed that STAT5B forms constitutively functional complexes with Gβγ subunits and the δ-OR. On the other hand, DSLET-activation of δ-OR, expressed in HEK293 cells, resulted in a PTX-dependent STAT5Β phosphorylation by a c-Src tyrosine kinase. Collectively, our results have shown the formation of dynamic complexes between STAT5B, Gβγ and δ-OR and reveal a novel signaling pathway through which δ-OR may modulate transcription in neurons and alter synaptosomal plasticity. |
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Αναφορές – References
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1. Levy D.E., Darnell J.E.,Jr: Stats: transcriptional control and biological impact. Nat. Rev. Mol. Cell Biol. 3: 651-662 (2002)
2. Ali M.S., Sayeski P.P., Bernstein K.E.: Jak2 acts as both a STAT1 kinase and as a molecular bridge linking STAT1 to the angiotensin II AT1 receptor. J. Biol. Chem. 275: 15586-15593 (2000) 3. Georgoussi Z.: Novel interacting partners regulating opioid receptor signaling. In: (Ciruela F., Lujan R., eds) Molecular Aspects of G Protein-Coupled Receptors. Chapter 6, pp. 169-206, Nova Science Publishers, Inc., 2008 4. Mazarakou G., Georgoussi Z.: STAT5A interacts with and is phosphorylated upon activation of the muopioid receptor. J. Neurochem. 93: 918-931 (2005) 5. Morou E., Gergoussi, Z.: Expression of the third intracellular loop of the delta-opioid receptor inhibits signaling by opioid receptors and other G protein-coupled receptors. J. Pharmacol. Exp. Ther. 315: 1368-1379 (2005) 6. Guillet-Deniau I., Burnol A.F., Girard J.: Identification and localization of a skeletal muscle secrotonin 5-HT2A receptor coupled to the Jak/STAT pathway. J. Biol. Chem. 272: 14825-14829 (1997) 7. Georgoussi Z., Leontiadis L., Mazarakou G., Merkouris M., Hyde K., Hamm H.: Selective interactions between G protein subunits and RGS4 with the C-terminal domains of the μ- and δ-opioid receptors regulate opioid receptor signalling. Cell. Signal. 18: 771-782 (2006) |
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Online ISSN 1011-6575
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Articles published in this Journal are Indexed or Abstracted in:
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• Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE
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Τι είναι η Επιθεώρηση Κλινικής Φαρμακολογίας και Φαρμακοκινητικής-Ελληνική Έκδοση-Οδηγίες προς τους Συγγραφείς
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Articles Published in Epitheorese Klinikes Farmakologias και Farmakokinetikes-Greek Edition
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