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      A potassium channel mutation in weaver mice implicates membrane excitability in granule cell differentiation.

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      Publication date:
      Journal: Nature genetics
      Keywords: Amino Acid Sequence, Animals, Base Sequence, Cell Differentiation, genetics, Cerebellum, cytology, physiology, Chromosome Mapping, Chromosomes, Human, Pair 21, Crosses, Genetic, DNA Primers, G Protein-Coupled Inwardly-Rectifying Potassium Channels, GTP-Binding Proteins, Gene Expression, Homozygote, Humans, Meiosis, Mice, Mice, Inbred C57BL, Mice, Neurologic Mutants, Molecular Sequence Data, Muridae, Neurons, Point Mutation, Polymerase Chain Reaction, Polymorphism, Genetic, Potassium Channels, chemistry, Potassium Channels, Inwardly Rectifying, Protein Structure, Secondary, Sequence Deletion, Sequence Homology, Amino Acid

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          Abstract

          Early events in neuronal differentiation are generally considered to be regulated by factors independent of alterations in membrane permeability. Weaver mice harbour a mutation that blocks neuronal differentiation just after cessation of cell division, prior to cell migration and synaptogenesis. Cerebellar granule cells in homozygous weaver mice fail to differentiate, either because intrinsic cues are absent or because the granule cells are unable to respond to those cues. We now report that weaver mice have a missense mutation in a gene encoding a G-protein coupled inward rectifier potassium channel. The mutation alters the putative ion-permeable, pore-forming domain of the protein, suggesting that granule cell differentiation is regulated by changes in membrane permeability.

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          A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels.

          T Abramson, R MacKinnon, L Heginbotham (1992)
          The overall sequence similarity between the voltage-activated K+ channels and cyclic nucleotide-gated ion channels from retinal and olfactory neurons suggests that they arose from a common ancestor. On the basis of sequence comparisons, mutations were introduced into the pore of a voltage-activated K+ channel. These mutations confer the essential features of ion conduction in the cyclic nucleotide-gated ion channels; the mutant K+ channels display little selectivity among monovalent cations and are blocked by divalent cations. The property of K+ selectivity is related to the presence of two amino acids that are absent from the pore-forming region of the cyclic nucleotide-gated channels. These data demonstrate that very small differences in the primary structure of an ion channel can account for extreme functional diversity, and they suggest a possible connection between the pore-forming regions of K+, Ca2+, and cyclic nucleotide-gated ion channels.
          Article 0 comments Cited 75 times – based on 0 reviews     Review now
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            Alteration of ionic selectivity of a K+ channel by mutation of the H5 region.

            D A Yool, T. Schwarz (1991)
            The high ionic selectivity of K+ channels is a unifying feature of this diverse class of membrane proteins. Though K+ channels differ widely in regulation and kinetics, physiological studies have suggested a common structure: a single file pore containing multiple ion-binding sites and having broader vestibules at both ends. We have used site-directed mutagenesis and single-channel recordings to identify a molecular region that influences ionic selectivity in a cloned A-type K+ channel from Drosophila. Single amino-acid substitutions in H5, the fifth hydrophobic region, enhanced the passage of NH4+ and Rb+, ions with diameters larger than K+, without compromising the ability of the channel to exclude the smaller cation, Na+. The mutations that substantially altered selectivity had little effect on the gating properties of the channel. We conclude that the H5 region is likely to line the pore of the K+ channel.
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              In situ labeling of granule cells for apoptosis-associated DNA fragmentation reveals different mechanisms of cell loss in developing cerebellum.

              Katherine A. Wood, Bruno Dipasquale, Richard Youle (1993)
              We have examined the role apoptosis plays during postnatal development of the mouse cerebellum by a new method utilizing T7 DNA polymerase for the in situ detection of DNA fragmentation associated with cell death. Granule cell loss between the third and fifth postnatal weeks, hypothesized to affect the granule cell to Purkinje cell stoichiometry, is not associated with DNA fragmentation. However, cerebellar granule cells undergo extensive nuclear DNA fragmentation between postnatal days 5 and 9. Cell death prior to synaptogenesis may help regulate granule cell number. Our results suggest that different mechanisms of cell death within the same neuronal cell population occur during development.
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                Author and article information

                Journal
                PubMed ID:: 7550338
                DOI:: 10.1038/ng1095-126

                ScienceOpen disciplines: Chemistry
                Keywords: Amino Acid Sequence,Animals,Base Sequence,Cell Differentiation,genetics,Cerebellum,cytology,physiology,Chromosome Mapping,Chromosomes, Human, Pair 21,Crosses, Genetic,DNA Primers,G Protein-Coupled Inwardly-Rectifying Potassium Channels,GTP-Binding Proteins,Gene Expression,Homozygote,Humans,Meiosis,Mice,Mice, Inbred C57BL,Mice, Neurologic Mutants,Molecular Sequence Data,Muridae,Neurons,Point Mutation,Polymerase Chain Reaction,Polymorphism, Genetic,Potassium Channels,chemistry,Potassium Channels, Inwardly Rectifying,Protein Structure, Secondary,Sequence Deletion,Sequence Homology, Amino Acid
                Data availability:
                ScienceOpen disciplines: Chemistry
                Keywords: Amino Acid Sequence, Animals, Base Sequence, Cell Differentiation, genetics, Cerebellum, cytology, physiology, Chromosome Mapping, Chromosomes, Human, Pair 21, Crosses, Genetic, DNA Primers, G Protein-Coupled Inwardly-Rectifying Potassium Channels, GTP-Binding Proteins, Gene Expression, Homozygote, Humans, Meiosis, Mice, Mice, Inbred C57BL, Mice, Neurologic Mutants, Molecular Sequence Data, Muridae, Neurons, Point Mutation, Polymerase Chain Reaction, Polymorphism, Genetic, Potassium Channels, chemistry, Potassium Channels, Inwardly Rectifying, Protein Structure, Secondary, Sequence Deletion, Sequence Homology, Amino Acid

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