A5043805019- Ion channel regulation and function
- Neuroscience and Neuropharmacology Research
- Erythrocyte Function and Pathophysiology
- Cardiac electrophysiology and arrhythmias
- Ion Channels and Receptors
- Nicotinic Acetylcholine Receptors Study
- Lipid Membrane Structure and Behavior
- Diverse Approaches in Healthcare and Education Studies
- Health and Wellbeing Research
- Circadian rhythm and melatonin
- Calcium signaling and nucleotide metabolism
- Bioactive Compounds and Antitumor Agents
- Electrochemical Analysis and Applications
- Neuroscience and Neural Engineering
- Pancreatic function and diabetes
- Ion Transport and Channel Regulation
- Receptor Mechanisms and Signaling
- Genetics, Aging, and Longevity in Model Organisms
- Cardiovascular, Neuropeptides, and Oxidative Stress Research
- bioluminescence and chemiluminescence research
- Cellular transport and secretion
- Medicinal Plants and Bioactive Compounds
Duke University
2024-2025
Daegu Gyeongbuk Institute of Science and Technology
2016-2024
Significance Lipids of bilayer membranes can segregate laterally into distinct liquid phases different composition called ordered and disordered, corresponding in the plasma membrane living cells to nanodomains raft nonraft domains. Using Förster resonance energy transfer genetically expressible protein probes lipid domains, we find that several steps metabolism phosphoinositide lipids are concentrated cholesterol-rich liquid-ordered domains membrane. The receptor-mediated breakdown...
Our sensory adaptation to cold and chemically induced coolness is mediated by the intrinsic property of TRPM8 channels desensitize. also implicated in cold-evoked pain disorders migraine, highlighting its inhibitors as an avenue for relief. Despite importance, mechanisms desensitization inhibition remained unclear. We found, using cryo–electron microscopy, electrophysiology, molecular dynamics simulations, that bind selectively desensitized state channel. These were used reveal overlapping...
Significance Transmembrane 16A (TMEM16A, anoctamin1), a Cl − channel activated by intracellular Ca 2+ and membrane voltage, displays several distinctive biophysical properties based on differential splicing of alternative exons. Recently, this was reported to be regulated the phospholipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ]. Here, we report that two splice variants TMEM16A show different PI(4,5)P sensitivity difference is related with presence or absence ATP. We reveal...
The β subunit of voltage-gated Ca2+ (CaV) channels plays an important role in regulating gating the α1 pore-forming and its regulation by phosphatidylinositol 4,5-bisphosphate (PIP2). Subcellular localization CaV is critical for this effect; N-terminal-dependent membrane targeting slows inactivation decreases PIP2 sensitivity. Here, we provide evidence that HOOK region biophysics. Based on amino acid composition, broadly divide into three domains: S (polyserine), A (polyacidic), B...
Significance Voltage-gated Ca 2+ (Ca V ) channels have an α1-α2δ core complexed with one of several alternative β subunits. Contradictory evidence says that, once bound, ( i a subunit is permanently associated the or ii that it free to be exchanged for other We designed rapamycin-translocatable subunits allow drug-induced sequestration organelle anchors. Sequestering does not dissociate bound from except when binding site mutated weaken interaction. Nevertheless, our rapamycin constructs...
Recently, we showed that the HOOK region of β2 subunit electrostatically interacts with plasma membrane and regulates current inactivation phosphatidylinositol 4,5-bisphosphate (PIP2) sensitivity voltage-gated Ca2+ (CaV) 2.2 channels. Here, report voltage-dependent gating density CaV2.2 channels are also regulated by subunit. The can be divided into 3 domains: S (polyserine), A (polyacidic), B (polybasic). We found domain shifted activation to more hyperpolarized depolarized voltages,...
High-voltage-activated Ca2+ (CaV) channels that adjust influx upon membrane depolarization are differentially regulated by phosphatidylinositol 4,5-bisphosphate (PIP2) in an auxiliary CaV β subunit-dependent manner. However, the molecular mechanism which subunits control PIP2 sensitivity of remains unclear. By engineering various α1B and constructs tsA-201 cells, we reported at least two PIP2-binding sites, including polybasic residues C-terminal end I-II loop binding pocket S4II domain,...
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