ArticleBiophysical journal2011
Tryptophan scanning mutagenesis of the first transmembrane domain of the innexin Shaking-B(Lethal).
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Innexin-Mediated Adhesion between Glia Is Required for Axon Ensheathment in the Peripheral Nervous System.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- A Limited and Diverse Set of Suppressor Mutations Restore Function to INX-8 Mutant Hemichannels in theBiomolecules · 2020Article
- NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.Developmental cell · 2020Article
- Probing the Structure of the HIV-1 Envelope Trimer Using Aspartate Scanning Mutagenesis.Journal of virology · 2020Article
- Integration of Migratory Cells into a New Site In Vivo Requires Channel-Independent Functions of Innexins on Microtubules.Developmental cell · 2020Article
- Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids.Science advances · 2020Article
- Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells.Chemical science · 2020Article
- The Transmembrane Domain of Synaptobrevin Influences Neurotransmitter Flux through Synaptic Fusion Pores.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Innexins: Expression, Regulation, and Functions.Frontiers in physiology · 2018Review
- Gap junction gene and protein families: Connexins, innexins, and pannexins.Biochimica et biophysica acta. Biomembranes · 2018Review
- Structure of an innexin gap junction channel and cryo-EM sample preparation.Microscopy (Oxford, England) · 2017Review
- Analysis of Large-Scale Mutagenesis Data To Assess the Impact of Single Amino Acid Substitutions.Genetics · 2017Article
- A structural and functional comparison of gap junction channels composed of connexins and innexins.Developmental neurobiology · 2017Review
- Atomic structure of the innexin-6 gap junction channel determined by cryo-EM.Nature communications · 2016Article
- Tryptophan Scanning Reveals Dense Packing of Connexin Transmembrane Domains in Gap Junction Channels Composed of Connexin32.The Journal of biological chemistry · 2015Article
- The pannexins: past and present.Frontiers in physiology · 2014Review
- Gap junction-dependent homolog avoidance in the developing CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Oligomeric structure and functional characterization of Caenorhabditis elegans Innexin-6 gap junction protein.The Journal of biological chemistry · 2013Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The channel proteins of gap junctions are encoded by two distinct gene families, connexins, which are exclusive to chordates, and innexins/pannexins, which are found throughout the animal kingdom. Although the relationship between the primary structure and function of the vertebrate connexins has been relatively well studied, there are, to our knowledge, no structure-function analyses of invertebrate innexins. In the first such study, we have used tryptophan scanning to probe the first transmembrane domain (M1) of the Drosophila innexin Shaking-B(Lethal), which is a component of rectifying electrical synapses in the Giant Fiber escape neural circuit. Tryptophan was substituted sequentially for 16 amino acids within M1 of Shaking-B(Lethal). Tryptophan insertion at every fourth residue (H27, T31, L35, and S39) disrupted gap junction function. The distribution of these sites is consistent with helical secondary structure and identifies the face of M1 involved in helix-helix interactions. Tryptophan substitution at several sites in M1 altered channel properties in a variety of ways. Changes in sensitivity to transjunctional voltage (Vj) were common and one mutation (S39W) induced sensitivity to transmembrane voltage (Vm). In addition, several mutations induced hemichannel activity. These changes are similar to those observed after substitutions within the transmembrane domains of connexins.
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