Journal
NATURE NEUROSCIENCE
Volume 13, Issue 1, Pages 69-U229Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nn.2454
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Funding
- Burroughs-Wellcome Fund
- US National Institutes of Health [K08NS059671, T32HL007953, R01GM057654, R01GM078579, P01AG017628, R01GM088221]
- University of Pennsylvania
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [T32HL007953] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM078579, R01GM057654, R01GM088221] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS072431, K08NS059671] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [P01AG017628] Funding Source: NIH RePORTER
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Sleep is a whole-organism phenomenon accompanied by global changes in neural activity. We previously identified SLEEPLESS (SSS) as a glycosylphosphatidyl inositol-anchored protein required for sleep in Drosophila. Here we found that SSS is critical for regulating the sleep-modulating potassium channel Shaker. SSS and Shaker shared similar expression patterns in the brain and specifically affected each other's expression levels. sleepless (sss) loss-of-function mutants exhibited altered Shaker localization, reduced Shaker current density and slower Shaker current kinetics. Transgenic expression of sss in sss mutants rescued defects in Shaker expression and activity cell-autonomously and suggested that SSS functions in wake-promoting, cholinergic neurons. In heterologous cells, SSS accelerated the kinetics of Shaker currents and was co-immunoprecipitated with Shaker, suggesting that SSS modulates Shaker activity via a direct interaction. SSS is predicted to belong to the Ly-6/neurotoxin superfamily, suggesting a mechanism for regulation of neuronal excitability by endogenous toxin-like molecules.
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