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doi:10.22028/D291-37174
Titel: | Expression of the C-Terminal Domain of Phospholipase Cβ3 Inhibits Signaling via Gαq-Coupled Receptors and Transient Receptor Potential Channels |
VerfasserIn: | Thiel, Gerald Rössler, Oliver G. |
Sprache: | Englisch |
Titel: | International Journal of Molecular Sciences |
Bandnummer: | 23 |
Heft: | 17 |
Verlag/Plattform: | MDPI |
Erscheinungsjahr: | 2022 |
Freie Schlagwörter: | Gαq-coupled designer receptor ERK1/2 m-3M3FBS phospholipase Cβ TRPM3 TRPM8 |
DDC-Sachgruppe: | 610 Medizin, Gesundheit |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | Transient receptor potential (TRP) channels are cation channels that play a regulatory role in pain and thermosensation, insulin secretion, and neurotransmission. It has been proposed that activation of TRP channels requires phosphatidylinositol 4,5-bisphosphate, the major substrate for phospholipase C (PLC). We investigated whether inhibition of PLCβ has an impact on TRP channel signaling. A genetic approach was used to avoid off-target effects observed when using a pharmacological PLCβ inhibitor. In this study, we show that expression of PLCβ1ct and PLCβ3ct, truncated forms of PLCβ1 or PLCβ3 that contain the C-terminal membrane binding domains, almost completely blocked the signal transduction of a Gαq-coupled designer receptor, including the phosphorylation of ERK1/2. In contrast, expression of the helix-turn-helix motif (Hα1—Hα2) of the proximal C-terminal domain of PLCβ3 did not affect Gαq-coupled receptor signaling. PLCβ3ct expression impaired signaling of the TRP channels TRPM3 and TRPM8, stimulated with either prognenolone sulfate or icilin. Thus, the C-terminal domain of PLCβ3 interacts with plasma membrane targets, most likely phosphatidylinositol 4,5-bisphosphate, and in this way blocks the biological activation of TRPM3 and TRPM8, which require interaction with this phospholipid. PLCβ thus regulates TRPM3 and TRPM8 channels by masking phosphatidylinositol 4,5-bisphosphate with its C-terminal domain. |
DOI der Erstveröffentlichung: | 10.3390/ijms23179590 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-371747 hdl:20.500.11880/33729 http://dx.doi.org/10.22028/D291-37174 |
ISSN: | 1422-0067 |
Datum des Eintrags: | 12-Sep-2022 |
Fakultät: | M - Medizinische Fakultät |
Fachrichtung: | M - Medizinische Biochemie und Molekularbiologie |
Professur: | M - Prof. Dr. Gerald Thiel |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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ijms-23-09590-v3.pdf | 2,42 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons