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in erregbaren als auch in nicht-erregbaren Zellen vorkommen. TRPC-Kanäle werden durch Diacylglycerol (DAG) aktiviert, ein Produkt, das im Phospholipase-C-(PLC)-Weg nach der Spaltung von Phosphatidylinositol-4,5-bisphosphat (PIP2) gebildet wird. Bemerkenswerterweise sind, obwohl alle TRPC-Kanäle an (patho)physiologischen Prozessen beteiligt sind, nur TRPC6 als ein Schlüsselfaktor in der Entwicklung einer schweren Nierenerkrankung bekannt, die als fokal segmentale Glomerulosklerose (FSGS) bezeichnet wird. FSGS ist durch einen kontinuierlichen Kalziumleckstrom durch TRPC6 gekennzeichnet, der das Ionen-Gleichgewicht in den glomerulären Zellen stört und letztendlich zu einer Glomerulosklerose führt. Jüngste kryo-elektronenmikroskopische (Kryo-EM) Studien von TRPC6 konnten nur Strukturen von geschlossenen Kanälen erfassen und geben keine Einblicke in die Dynamik des Kanalöffnungsmechanismus, selbst in Anwesenheit von Aktivatoren. Ein Verständnis des Öffnungsmechanismus des TRPC6-Kanals zu gewinnen, wird jedoch unser Verständnis seiner pathophysiologischen Bedeutung erweitern. Darüber hinaus wird es die Grundlage für die Entwicklung pharmakologischer Strategien zur Regulierung des Kanals in nativen Geweben schaffen. Elektrophysiologische Analysen des TRPC6-Verhaltens auf Einzelkanalebene zeigten einen kurzlebigen geöffneten Zustand des Kanals. Folglich vermuten wir, dass das Kanalverhalten das Haupthindernis beim Verständnis des Öffnungsmechanismus von TRPC6-Kanälen in Kryo-EM-Studien darstellt. Hochgeschwindigkeits-Atomkraftmikroskopie (HS-AFM), eine hochmoderne Technik, hat in den letzten Jahren insbesondere bei der Untersuchung der Kanalöffnungsmechanismen von Ionenkanälen viel Aufmerksamkeit erlangt. Diese Technik ermöglicht hochauflösende und zeitlich aufgelöste topografische Bilder einer Probe, indem ihre Oberfläche gescannt wird. Kürzlich hat die Gruppe von Prof. Dr. Scheuring erfolgreich HS-AFM eingesetzt, um die Dynamik in den TRPV2- und TRPV3-Kanälen zu untersuchen. Um ein umfassendes Verständnis von TRPC6 zu erlangen und das Verhalten des Kanals in nativem Gewebe zu verstehen, werden wir die Dynamik des Kanalöffnungsmechanismus nach Stimulation mit verschiedenen Agonisten unter Verwendung von HS-AFM untersuchen.","en":"Transient receptor potential canonical (TRPC) channels are calcium permeable ion channels found both in excitable and non-excitable cells. TRPC channels are activated by diacylglycerol (DAG), a product generated in the phospholipase C (PLC) pathway following the cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2). Notably, although all TRPC channels are involved in (patho)physiological processes, only TRPC6 has been identified as playing a pivotal role in the development of a severe kidney disease known as focal segmental glomerulosclerosis (FSGS). FSGS is characterized by continuous calcium leakage through TRPC6, which disturbs ion homeostasis within glomerular cells, ultimately resulting in glomerular sclerosis. Recent cryo-electron microscopy (cryo-EM) studies of TRPC61–3 could obtain only closed-channel structures and do not give insights into the dynamics of channel gating even in presence of activators. However, gaining an understanding of the gating mechanism of the TRPC6 channel will enhance our comprehension of its pathophysiological significance. Furthermore, it will establish a foundation for developing pharmacological strategies to regulate the channel within native tissues. Electrophysiological analysis of TRPC6 behavior on a single channel level showed a short-lived open state of the channel.4 Consequently, we hypothesized that the channel behavior is the main obstacle in gaining insights into the gating mechanism of TRPC6 channels during cryo-EM.  High-speed atomic force microscopy (HS-AFM), a state-of-the-art technique, has gained high attention in recent years especially in studying ion channel gating. This technique allows high-resolution and time resolved topographic images of a sample by scanning its surface. Recently the group of Prof. Dr. Scheuring, successfully employed HS-AFM to study the dynamics in TRPV25 and TRPV36 ion channels. To gain a comprehensive understanding of TRPC6 and understand the behavior of the channel in native tissue we will study the dynamics of channel gating upon stimulation with different agonists using HS-AFM. 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