TRPM4是一种Ca2+激活的非选择性离子通道,介导细胞膜脱极化
Pierre Launay1, Andrea Fleig, Anne Laure Perraud
1Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
Cell
|May 23, 2002
概括
研究人员确定TRPM4b是一种激活的非选择性 (CAN) 阴离子通道. 这个TRP通道通过调节各种细胞类型的膜潜力来调节的流入.
科学领域:
- 分子生物学分子生物学
- 细胞生理细胞生理学
- 离子通道功能 离子通道功能
背景情况:
- 激活的非选择性 (CAN) 阴离子通道对于神经元活动和液体分泌等细胞功能至关重要.
- TRP通道是一个多样化的家族,参与感知各种刺激.
研究的目的:
- 识别和描述一个CAN通道的分子候选.
- 研究TRPM4b在细胞信号传递中的作用.
主要方法:
- 克隆和特征TRPM4b基因.
- 电生理学记录以确定通道特性 (导电,离子选择性,激活动力学).
- 对TRPM4b激活的分析,以响应受体介导的动员.
主要成果:
- TRPM4b编码了一个带有25 pS单元导电率的阴离子通道.
- TRPM4b是由细胞内 ([Ca2+]i) 直接激活的,其K (D) 值为400nm.
- 该通道传导Na +和K +,但不是Ca2 +,并且由受体介导的增加激活.
结论:
- TRPM4b是CAN通道的一个分子候选.
- 通过影响膜潜能,TRPM4b在流入中起着调节作用.
- 这种机制调节了通过其他途径进入的驱动力.
更多相关视频
相关概念视频
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...
Mechanically-gated Ion Channels
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
G-Protein Gated Ion Channels
GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
Sensory organs,...
IP3/DAG Signaling Pathway
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...


