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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

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