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Recent structures of the potassium channel provide an essential beginning point for explaining how the pore is gated between open and closed conformations by changes in membrane voltage. Yet, the molecular details of this process and the connections to transmembrane gradients are not understood. To begin addressing how changes within a membrane environment lead to the channel's ability to sense shifts in membrane voltage and to gate, we performed double-bilayer simulations of the Kv1.2 channel. These double-bilayer simulations enable us to simulate realistic voltage drops from resting potential conditions to depolarized conditions by changes in the bath conditions on each side of the bilayer. Our results show how the voltage sensor domain movement responds to differences in transmembrane potential. The initial voltage sensor domain movement, S4 in particular, is modulated by the gating charge response to changes in voltage and is initially stabilized by the lipid headgroups. We show this response is directly coupled to the initial stages of pore domain motion. Results presented here provide a molecular model for how the pre-gating process occurs in sequential steps: Gating charge response, movement and stabilization of the S4 voltage sensor domain, and movement near the base of the S5 region to close the pore domain.
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http://dx.doi.org/10.3109/09687680903278539 | DOI Listing |
Stem Cell Reports
September 2025
Neural Stem Cells and Neuroimaging Group, Department of Neurobiology, Hellenic Pasteur Institute, 11521 Athens, Greece. Electronic address:
In the adult brain, neural stem cells (NSCs) constitutively generate new neurons in specific neurogenic domains. Recent research has unveiled reactive neurogenesis, whereby brain injury triggers NSC activation, enhancing their differentiation potential and guiding progeny to injured areas. Our study provides evidence of alternative migration pathways for newborn neurons in the mouse subcortical forebrain, revealed by administration of a chemotherapeutic agent.
View Article and Find Full Text PDFmBio
September 2025
School of Biological Sciences, University of Auckland, Auckland, New Zealand.
The rotation of the bacterial flagellum is powered by the MotAB stator complex, which converts ion flux into torque. Despite its central role in flagellar function, the evolutionary origin and structural diversity of this system remain poorly understood. Here, we present the first comprehensive phylogenetic and structural characterization of MotAB and its closest non-flagellar homologs.
View Article and Find Full Text PDFBMC Neurol
September 2025
Department of Neurology, University Hospital Schleswig-Holstein, Kiel, Germany.
Background: Parkinson's disease (PD) is characterized by motor symptoms altering gait domains such as slow walking speed, reduced step and stride length, and increased double support time. Gait disturbances occur in the early, mild to moderate, and advanced stages of the disease in both backward walking (BW) and forward walking (FW), but are more pronounced in BW. At this point, however, no information is available about BW performance and disease stages specified using the Hoehn and Yahr (H&Y) scale.
View Article and Find Full Text PDFSci China Life Sci
September 2025
MOE Key Laboratory of Bioinformatics and Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Tomato brown rugose fruit virus (ToBRFV) overcomes all known tomato resistance genes, including the durable Tm-2, posing a serious threat to global tomato production. Here, we employed in vitro random mutagenesis to evolve the Tm-2 leucine-rich repeat (LRR) domain and screened ∼8,000 variants for gain-of-function mutants capable of recognizing the ToBRFV movement protein (MP) and triggering hypersensitive cell death. We identified five such mutants.
View Article and Find Full Text PDFCurr Biol
September 2025
Department of Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616, USA. Electronic address:
Nuclear migration plays a fundamental role in development, requiring precise spatiotemporal control of bidirectional movement through dynein and kinesin motors. Here, we uncover a differential isoform-dependent mechanism for developmental regulation of nuclear migration directionality. The nuclear envelope Klarsicht/ANC-1/Syne homology (KASH) protein UNC-83 in Caenorhabditis elegans exists in multiple isoforms that differentially control motor activity to achieve tissue-specific nuclear positioning.
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