TRPC7.
1Laboratory of Molecular Biology, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, 615-8510 Kyoto, Japan.
Handbook of Experimental Pharmacology
|January 16, 2007
Summary
Canonical transient receptor potential7 (TRPC7) channels are activated by diacylglycerol (DAG) and show unique calcium regulation. Further research is needed to understand TRPC7
Area of Science:
- Molecular Biology
- Cell Physiology
- Ion Channel Function
Background:
- Canonical transient receptor potential7 (TRPC7) belongs to the mammalian TRPC channel family.
- TRPC channels are nonselective cation channels activated via the phospholipase C (PLC) signaling pathway.
- TRPC7 shares homology with TRPC3 and TRPC6, also activated by diacylglycerol (DAG).
Purpose of the Study:
- To investigate the activation mechanisms and properties of TRPC7.
- To explore the unique characteristics of TRPC7, including its constitutive activity and regulation by extracellular calcium (Ca2+).
- To elucidate the potential physiological roles of TRPC7 in native cellular environments and calcium signaling pathways.
Main Methods:
- Analysis of TRPC7 sequence homology with related TRPC channels (TRPC3, TRPC6).
- Investigation of TRPC7 activation by diacylglycerol (DAG).
- Characterization of TRPC7's unique activation properties, including constitutive activity and negative regulation by extracellular Ca2+.
Main Results:
- TRPC7 is directly activated by diacylglycerol (DAG), a product of PLC signaling.
- TRPC7 exhibits constitutive activity, meaning it can be active without a direct external stimulus.
- Extracellular calcium (Ca2+) negatively regulates TRPC7 activity.
Conclusions:
- TRPC7 possesses distinct activation properties compared to other TRPC channels.
- The unique features of TRPC7, including its constitutive activity and calcium-dependent regulation, suggest significant roles in cellular calcium signaling.
- Further investigation is warranted to fully understand the physiological importance of TRPC7 in native systems.
Related Concept Videos
Thermosensation
Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
Repressible Operon: trp Operon
The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
G-protein Coupled Receptors
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
G Protein-coupled Receptors
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs Regulate Adenylyl Cylase Activity
Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
Two...

