Activity-dependent Golgi satellite formation in dendrites reshapes the neuronal surface glycoproteome
| Autor: | Okunola Jeyifous, Zola Yi, Luke Newell, Aubrey V. Weigel, Theron A. Russell, William Ramos, Geoffrey T. Swanson, Jason C. Casler, Abhijit Ramaprasad, Jing-Zhi Yan, Benjamin S. Glick, Fernando M. Valbuena, Anitha P. Govind, William N. Green, Jennifer Lippincott-Schwartz |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proteome
Endocytic cycle Golgi Apparatus Receptors Nicotinic Endoplasmic Reticulum Autoantigens neuronal activity Golgi Premovement neuronal activity Biology (General) Neurons Membrane Glycoproteins Chemistry General Neuroscience General Medicine Cell biology medicine.anatomical_structure sialic acid symbols Medicine Research Article Human glycosylation Endosome QH301-705.5 Science Dendrite General Biochemistry Genetics and Molecular Biology symbols.namesake Neurotransmitter receptor Polysaccharides medicine Animals Humans Golgi satellites Secretory pathway Cell Proliferation General Immunology and Microbiology Endoplasmic reticulum Membrane Proteins Dendrites Cell Biology Golgi apparatus Rats HEK293 Cells Rat Neuroscience nicotine |
| Zdroj: | eLife, Vol 10 (2021) eLife |
| Popis: | Activity-driven changes in the neuronal surface glycoproteome are known to occur with synapse formation, plasticity, and related diseases, but their mechanistic basis and significance are unclear. Here, we observed that N-glycans on surface glycoproteins of dendrites shift from immature to mature forms containing sialic acid in response to increased neuronal activation. In exploring the basis of these N-glycosylation alterations, we discovered that they result from the growth and proliferation of Golgi satellites scattered throughout the dendrite. Golgi satellites that formed during neuronal excitation were in close association with endoplasmic reticulum (ER) exit sites and early endosomes and contained glycosylation machinery without the Golgi structural protein, GM130. They functioned as distal glycosylation stations in dendrites, terminally modifying sugars either on newly synthesized glycoproteins passing through the secretory pathway or on surface glycoproteins taken up from the endocytic pathway. These activities led to major changes in the dendritic surface of excited neurons, impacting binding and uptake of lectins, as well as causing functional changes in neurotransmitter receptors such as nicotinic acetylcholine receptors. Neural activity thus boosts the activity of the dendrite’s satellite micro-secretory system by redistributing Golgi enzymes involved in glycan modifications into peripheral Golgi satellites. This remodeling of the neuronal surface has potential significance for synaptic plasticity, addiction, and disease. |
| Databáze: | OpenAIRE |
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