title: Nanos-mediated repression of hid protects larval sensory neurons after a global switch in sensitivity to apoptotic signals.
abstract: Dendritic arbor morphology is a key determinant of neuronal function. Once established, dendrite branching patterns must be maintained as the animal develops to ensure receptive field coverage. The translational repressors Nanos (Nos) and Pumilio (Pum) are required to maintain dendrite growth and branching of Drosophila larval class IV dendritic arborization (da) neurons, but their specific regulatory role remains unknown. We show that Nos-Pum-mediated repression of the pro-apoptotic gene head involution defective (hid) is required to maintain a balance of dendritic growth and retraction in class IV da neurons and that upregulation of hid results in decreased branching because of an increase in caspase activity. The temporal requirement for nos correlates with an ecdysone-triggered switch in sensitivity to apoptotic stimuli that occurs during the mid-L3 transition. We find that hid is required during pupariation for caspase-dependent pruning of class IV da neurons and that Nos and Pum delay pruning. Together, these results suggest that Nos and Pum provide a crucial neuroprotective regulatory layer to ensure that neurons behave appropriately in response to developmental cues.
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Balpreet
authors.initials: B
authors.lastname: Bhogal
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Amara
authors.initials: A
authors.lastname: Plaza-Jennings
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA gavis@princeton.edu.
authors.forename: Elizabeth R
authors.identifier: 0000-0003-0251-0760
authors.initials: ER
authors.lastname: Gavis
mesh_terms: D020413:3' Untranslated Regions / Q000235:genetics; D000818:Animals; D017209:Apoptosis; D020169:Caspases / Q000378:metabolism; D019610:Cytoprotection; D003712:Dendrites / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D004440:Ecdysone / Q000378:metabolism; D007814:Larva / Q000166:cytology / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D009154:Mutation / Q000235:genetics; D009479:Neuropeptides / Q000378:metabolism*; D010641:Phenotype; D011485:Protein Binding; D011679:Pupa / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D011984:Sensory Receptor Cells / Q000166:cytology* / Q000378:metabolism*; D015398:Signal Transduction; D015854:Up-Regulation / Q000235:genetics
chemical_list: D020413:3' Untranslated Regions; D029721:Drosophila Proteins; C108880:HID protein, Drosophila; D009479:Neuropeptides; D016601:RNA-Binding Proteins; C074333:pum protein, Drosophila; C070574:nos protein, Drosophila; D004440:Ecdysone; D020169:Caspases
keywords: Caspase; Drosophila; Non-apoptotic function; Nos; da neurons; hid