Unconventional secretory processing diversifies neuronal ion channel properties.
Autor: | Hanus C; Max Planck Institute for Brain Research, Frankfurt, Germany., Geptin H; Max Planck Institute for Brain Research, Frankfurt, Germany., Tushev G; Max Planck Institute for Brain Research, Frankfurt, Germany., Garg S; Max Planck Institute for Brain Research, Frankfurt, Germany., Alvarez-Castelao B; Max Planck Institute for Brain Research, Frankfurt, Germany., Sambandan S; Max Planck Institute for Brain Research, Frankfurt, Germany., Kochen L; Max Planck Institute for Brain Research, Frankfurt, Germany., Hafner AS; Max Planck Institute for Brain Research, Frankfurt, Germany., Langer JD; Max Planck Institute for Brain Research, Frankfurt, Germany.; Max Planck Institute for Biophysics, Frankfurt, Germany., Schuman EM; Max Planck Institute for Brain Research, Frankfurt, Germany. |
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Jazyk: | angličtina |
Zdroj: | ELife [Elife] 2016 Sep 28; Vol. 5. Date of Electronic Publication: 2016 Sep 28. |
DOI: | 10.7554/eLife.20609 |
Abstrakt: | 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. Competing Interests: The authors declare that no competing interests exist. |
Databáze: | MEDLINE |
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