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  Unconventional secretory processing diversifies neuronal ion channel properties

Hanus, C., Geptin, H., Tushev, G., Garg, S., Alvarez-Castelao, B., Sambandan, S., et al. (2016). Unconventional secretory processing diversifies neuronal ion channel properties. Elife, 5. doi:10.7554/eLife.20609.

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Hanus, C., Author
Geptin, H., Author
Tushev, G., Author
Garg, S., Author
Alvarez-Castelao, B., Author
Sambandan, S., Author
Kochen, L., Author
Hafner, A. S., Author
Langer, J. D., Author
Schuman, Erin M.1, Author           
Affiliations:
1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              

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Free keywords: Animals Brain Chemistry Cell Line *Glycosylation Immunoblotting Ion Channels/*metabolism Mammals Mass Spectrometry Membrane Proteins/metabolism Neurons/*chemistry Optical Imaging *cell biology *golgi-bypass *neuronal membrane proteins *neuroscience *rat
 Abstract: N-glycosylation - the sequential addition of complex sugars to adhesion proteins, neurotransmitter receptors, ion channels and secreted trophic factors as they progress through the endoplasmic reticulum and the Golgi apparatus - is one of the most frequent protein modifications. In mammals, most organ-specific N-glycosylation events occur in the brain. Yet, little is known about the nature, function and regulation of N-glycosylation in neurons. Using imaging, quantitative immunoblotting and mass spectrometry, we show that hundreds of neuronal surface membrane proteins are core-glycosylated, resulting in the neuronal membrane displaying surprisingly high levels of glycosylation profiles that are classically associated with immature intracellular proteins. We report that while N-glycosylation is generally required for dendritic development and glutamate receptor surface expression, core-glycosylated proteins are sufficient to sustain these processes, and are thus functional. This atypical glycosylation of surface neuronal proteins can be attributed to a bypass or a hypo-function of the Golgi apparatus. Core-glycosylation is regulated by synaptic activity, modulates synaptic signaling and accelerates the turnover of GluA2-containing glutamate receptors, revealing a novel mechanism that controls the composition and sensing properties of the neuronal membrane.

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 Dates: 2016-10-25
 Publication Status: Issued
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 Identifiers: Other: 27677849
DOI: 10.7554/eLife.20609
ISSN: 2050-084X (Electronic)2050-084X (Linking)
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Title: Elife
Source Genre: Journal
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Pages: - Volume / Issue: 5 Sequence Number: - Start / End Page: - Identifier: -