title: Staufen- and FMRP-containing neuronal RNPs are structurally and functionally related to somatic P bodies.
abstract: Local control of mRNA translation modulates neuronal development, synaptic plasticity, and memory formation. A poorly understood aspect of this control is the role and composition of ribonucleoprotein (RNP) particles that mediate transport and translation of neuronal RNAs. Here, we show that staufen- and FMRP-containing RNPs in Drosophila neurons contain proteins also present in somatic "P bodies," including the RNA-degradative enzymes Dcp1p and Xrn1p/Pacman and crucial components of miRNA (argonaute), NMD (Upf1p), and general translational repression (Dhh1p/Me31B) pathways. Drosophila Me31B is shown to participate (1) with an FMRP-associated, P body protein (Scd6p/trailer hitch) in FMRP-driven, argonaute-dependent translational repression in developing eye imaginal discs; (2) in dendritic elaboration of larval sensory neurons; and (3) in bantam miRNA-mediated translational repression in wing imaginal discs. These results argue for a conserved mechanism of translational control critical to neuronal function and open up new experimental avenues for understanding the regulation of mRNA function within neurons.
authors.affiliation: Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Barbee
authors.forename: Patricia S
authors.initials: PS
authors.lastname: Estes
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Cziko
authors.forename: Jens
authors.initials: J
authors.lastname: Hillebrand
authors.forename: Rene A
authors.initials: RA
authors.lastname: Luedeman
authors.forename: Jeff M
authors.initials: JM
authors.lastname: Coller
authors.forename: Nick
authors.initials: N
authors.lastname: Johnson
authors.forename: Iris C
authors.initials: IC
authors.lastname: Howlett
authors.forename: Cuiyun
authors.initials: C
authors.lastname: Geng
authors.forename: Ryu
authors.initials: R
authors.lastname: Ueda
authors.forename: Andrea H
authors.initials: AH
authors.lastname: Brand
authors.forename: Sarah F
authors.initials: SF
authors.lastname: Newbury
authors.forename: James E
authors.initials: JE
authors.lastname: Wilhelm
authors.forename: Richard B
authors.initials: RB
authors.lastname: Levine
authors.forename: Akira
authors.initials: A
authors.lastname: Nakamura
authors.forename: Roy
authors.initials: R
authors.lastname: Parker
authors.forename: Mani
authors.initials: M
authors.lastname: Ramaswami
mesh_terms: D000818:Animals; D030801:Animals, Genetically Modified; D015152:Blotting, Northern; D015153:Blotting, Western / Q000379:methods; D020169:Caspases / Q000378:metabolism; D002478:Cells, Cultured; D002490:Central Nervous System / Q000166:cytology; D003712:Dendrites / Q000378:metabolism / Q000502:physiology; D004330:Drosophila; D029721:Drosophila Proteins / Q000378:metabolism / Q000502:physiology*; D005095:Exoribonucleases / Q000378:metabolism; D005123:Eye / Q000378:metabolism / Q000648:ultrastructure; D051860:Fragile X Messenger Ribonucleoprotein 1 / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000378:metabolism; D007150:Immunohistochemistry / Q000379:methods; D007814:Larva; D035683:MicroRNAs / Q000378:metabolism; D008855:Microscopy, Electron, Scanning / Q000379:methods; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000502:physiology; D021381:Protein Transport / Q000502:physiology; D016601:RNA-Binding Proteins / Q000378:metabolism*; D034743:RNA-Induced Silencing Complex / Q000378:metabolism; D012261:Ribonucleoproteins / Q000502:physiology*
chemical_list: D020169:Caspases; D029721:Drosophila Proteins; D005095:Exoribonucleases; D051860:Fragile X Messenger Ribonucleoprotein 1; D049452:Green Fluorescent Proteins; D035683:MicroRNAs; D016601:RNA-Binding Proteins; D034743:RNA-Induced Silencing Complex; D012261:Ribonucleoproteins; C069927:stau protein, Drosophila; C487208:pcm protein, Drosophila; C103568:Dcp-1 protein, Drosophila