Neuronal programmed cell death induces glial cell division in the adult Drosophila brain.
Although mechanisms that lead to programmed cell death (PCD) in neurons have been analysed extensively, little is known about how surrounding cells coordinate with it. Here we show that neuronal PCD in the Drosophila brain induces glial cell division. We identified PCD in neurons and cell division in glia occurring in a consistent spatiotemporal manner in adult flies shortly after eclosion. Glial division was suppressed when neuronal PCD was inhibited by ectopic expression of the caspase inhibitor gene p35, indicating their causal relationship. Glia also responded to neural injury in a similar manner: both stab injury and degeneration of sensory axons in the brain caused by antennal ablation induced glial division. Eiger, a tumour necrosis factor superfamily ligand, appears to be a link between developmental PCD/neural injury and glial division, as glial division was attenuated in eiger mutant flies. Whereas PCD soon after eclosion occurred in eiger mutants as in the wild type, we observed excess neuronal PCD 2 days later, suggesting a protective function for Eiger or the resulting glial division against the endogenous PCD. In older flies, between 6 and 50 days after adult eclosion, glial division was scarcely observed in the intact brain. Moreover, 8 days after adult eclosion, glial cells no longer responded to brain injury. These results suggest that the life of an adult fly can be divided into two phases: the first week, as a critical period for neuronal cell death-associated glial division, and the remainder.
Kato
Kentaro
K
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. k.kato@bham.ac.uk
Awasaki
Takeshi
T
Ito
Kei
K
D000818:Animals; D017209:Apoptosis; D001369:Axons / Q000378:metabolism / Q000473:pathology; D001921:Brain / Q000166:cytology* / Q000473:pathology; D002455:Cell Division; D029721:Drosophila Proteins / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology* / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D018978:Molting; D009457:Neuroglia / Q000166:cytology* / Q000378:metabolism; D009474:Neurons / Q000166:cytology* / Q000378:metabolism
D029721:Drosophila Proteins; D008565:Membrane Proteins; C464573:egr protein, Drosophila