ArticleThe Journal of general physiology2009
Conformational changes in a pore-forming region underlie voltage-dependent "loop gating" of an unapposed connexin hemichannel.
Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 64 citations in OpenAlex.
- Influence of extracellular magnesium ions on the functional state and biophysical and structural properties of connexin36 hemichannels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- An Ala/Glu difference in E1 of Cx26 and Cx30 contributes to their differential anionic permeabilities.The Journal of general physiology · 2024Article
- A pore locus in the E1 domain differentially regulates Cx26 and Cx30 hemichannel function.The Journal of general physiology · 2024Article
- Electrical coupling and its channels.The Journal of general physiology · 2018Review
- Gating of Connexin Channels by transjunctional-voltage: Conformations and models of open and closed states.Biochimica et biophysica acta. Biomembranes · 2018Review
- Cues to Opening Mechanisms FromFrontiers in molecular neuroscience · 2018Article
- Permeant-specific gating of connexin 30 hemichannels.The Journal of biological chemistry · 2017Article
- Calcium binding and voltage gating in Cx46 hemichannels.Scientific reports · 2017Article
- The NHAmerican journal of physiology. Cell physiology · 2017Article
- Accessing gap-junction channel structure-function relationships through molecular modeling and simulations.BMC cell biology · 2017Review
- Gap junction structure: unraveled, but not fully revealed.F1000Research · 2017Review
- Charged Residues at the First Transmembrane Region Contribute to the Voltage Dependence of the Slow Gate of Connexins.The Journal of biological chemistry · 2016Article
- Syndromic deafness mutations at Asn 14 differentially alter the open stability of Cx26 hemichannels.The Journal of general physiology · 2016Article
- Connexinopathies: a structural and functional glimpse.BMC cell biology · 2016Review
- Computational Studies of Molecular Permeation through Connexin26 Channels.Biophysical journal · 2016Article
- An electrostatic mechanism for Ca(2+)-mediated regulation of gap junction channels.Nature communications · 2016Article
- Carbon Monoxide Modulates Connexin Function through a Lipid Peroxidation-Dependent Process: A Hypothesis.Frontiers in physiology · 2016Article
- Glutathione release through connexin hemichannels: Implications for chemical modification of pores permeable to large molecules.The Journal of general physiology · 2015Article
- Aberrant connexin26 hemichannels underlying keratitis-ichthyosis-deafness syndrome are potently inhibited by mefloquine.The Journal of investigative dermatology · 2015Article
- Control of the neurovascular coupling by nitric oxide-dependent regulation of astrocytic Ca(2+) signaling.Frontiers in cellular neuroscience · 2015Review
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4 authors at 2 institutions in 1 country.
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Abstract
The structure of the pore is critical to understanding the molecular mechanisms underlying selective permeation and voltage-dependent gating of channels formed by the connexin gene family. Here, we describe a portion of the pore structure of unapposed hemichannels formed by a Cx32 chimera, Cx32*Cx43E1, in which the first extracellular loop (E1) of Cx32 is replaced with the E1 of Cx43. Cysteine substitutions of two residues, V38 and G45, located in the vicinity of the border of the first transmembrane (TM) domain (TM1) and E1 are shown to react with the thiol modification reagent, MTSEA-biotin-X, when the channel resides in the open state. Cysteine substitutions of flanking residues A40 and A43 do not react with MTSEA-biotin-X when the channel resides in the open state, but they react with dibromobimane when the unapposed hemichannels are closed by the voltage-dependent "loop-gating" mechanism. Cysteine substitutions of residues V37 and A39 do not appear to be modified in either state. Furthermore, we demonstrate that A43C channels form a high affinity Cd2+ site that locks the channel in the loop-gated closed state. Biochemical assays demonstrate that A43C can also form disulfide bonds when oocytes are cultured under conditions that favor channel closure. A40C channels are also sensitive to micromolar Cd2+ concentrations when closed by loop gating, but with substantially lower affinity than A43C. We propose that the voltage-dependent loop-gating mechanism for Cx32*Cx43E1 unapposed hemichannels involves a conformational change in the TM1/E1 region that involves a rotation of TM1 and an inward tilt of either each of the six connexin subunits or TM1 domains.
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