title: Kismet positively regulates glutamate receptor localization and synaptic transmission at the Drosophila neuromuscular junction.
abstract: The Drosophila neuromuscular junction (NMJ) is a glutamatergic synapse that is structurally and functionally similar to mammalian glutamatergic synapses. These synapses can, as a result of changes in activity, alter the strength of their connections via processes that require chromatin remodeling and changes in gene expression. The chromodomain helicase DNA binding (CHD) protein, Kismet (Kis), is expressed in both motor neuron nuclei and postsynaptic muscle nuclei of the Drosophila larvae. Here, we show that Kis is important for motor neuron synaptic morphology, the localization and clustering of postsynaptic glutamate receptors, larval motor behavior, and synaptic transmission. Our data suggest that Kis is part of the machinery that modulates the development and function of the NMJ. Kis is the homolog to human CHD7, which is mutated in CHARGE syndrome. Thus, our data suggest novel avenues of investigation for synaptic defects associated with CHARGE syndrome.
authors.affiliation: Department of Biology, Drexel University, Philadelphia, Pennsylvania, United States of America.
authors.forename: Rupa
authors.initials: R
authors.lastname: Ghosh
authors.affiliation: Department of Biology, Drexel University, Philadelphia, Pennsylvania, United States of America.
authors.forename: Srikar
authors.initials: S
authors.lastname: Vegesna
authors.affiliation: Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, Illinois, United States of America.
authors.forename: Ramia
authors.initials: R
authors.lastname: Safi
authors.affiliation: Division of Biological Sciences, University of Missouri, Columbia, Missouri, United States of America.
authors.forename: Hong
authors.initials: H
authors.lastname: Bao
authors.affiliation: Division of Biological Sciences, University of Missouri, Columbia, Missouri, United States of America.
authors.forename: Bing
authors.initials: B
authors.lastname: Zhang
authors.affiliation: Department of Biology, Drexel University, Philadelphia, Pennsylvania, United States of America; Department of Neurobiology and Anatomy, Drexel University College of Medicine, Philadelphia, Pennsylvania, United States of America.
authors.forename: Daniel R
authors.initials: DR
authors.lastname: Marenda
authors.affiliation: Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, Illinois, United States of America.
authors.forename: Faith L W
authors.initials: FL
authors.lastname: Liebl
mesh_terms: D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D004265:DNA Helicases / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D004330:Drosophila / Q000254:growth & development / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000378:metabolism*; D007150:Immunohistochemistry; D007814:Larva / Q000378:metabolism; D008124:Locomotion / Q000502:physiology; D009046:Motor Neurons / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D009469:Neuromuscular Junction / Q000378:metabolism*; D017470:Receptors, Glutamate / Q000378:metabolism*; D013569:Synapses / Q000378:metabolism / Q000473:pathology; D009435:Synaptic Transmission / Q000502:physiology*
chemical_list: D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D018398:Homeodomain Proteins; D017470:Receptors, Glutamate; D004265:DNA Helicases; C118474:kis protein, Drosophila