Impaired N-Glycosylation Processing Impacts Neuronal Function
type: CreativeWork
description: Modifications of membrane proteins are carried out primarily using N-linked glycosylation. N-glycosylation has the potential to co-translationally and post-translationally modify protein function by the addition and processing of oligosaccharides. These oligosaccharides are known as glycans and are broken up into three types: oligomannose, hybrid and complex. Modification of oligosaccharides is performed by enzymes known as N-acetylglucosaminyltransferases (GnTs). Encoding of GnT proteins is performed by genes known as Mgats. Kv3.1b is an alpha subunit of a voltage-gated potassium channel known as Kv3 channels. Kv3 channels have the ability to open and close much more rapidly than other K channels, thus allowing neurons to create trains of action potentials. Kv3.1b is N-glycosylated at two sites, the N220 site and N229. The first aim of this study was to examine caudal primary (CaP) motor neuron development and the motor activity of WT AB larval zebrafish when the N220 site of a Kv3.1b alpha subunit is abolished. The zebrafish expressing N220Q Kv3.1b protein in CaP motor neuron displayed maldeveloped CaP neurons and a significant reduction in motor activity throughout larval development compared to those expressing Wt Kv3.1b protein or EGFP in CaP neurons. The second aim was to determine the effect of atypical N-glycosylation processing in developing zebrafish. Herein, CRISPR/Cas9 was implemented to create the Mgat1b -/-and Mgat1a -/- fish strains for current and future experiments. Mgat1 genes are responsible for the encoding of GnT enzymes. The Mgat1b -/- strain has increased oligomannose type glycans, as demonstrated by the Galanthus Nivalis Lectin (GNL) lectin binding assay. Up until now, the Mgat1b strain has been established, while the Mgat1a strain is still in progress. The locomotor studies indicated that the Mgat1b -/- strain is less active than the WT AB strain. The confocal images suggest cell morphology of CaP neurons are lacking branches. The third and …
abstract: Modifications of membrane proteins are carried out primarily using N-linked glycosylation. N-glycosylation has the potential to co-translationally and post-translationally modify protein function by the addition and processing of oligosaccharides. These oligosaccharides are known as glycans and are broken up into three types: oligomannose, hybrid and complex. Modification of oligosaccharides is performed by enzymes known as N-acetylglucosaminyltransferases (GnTs). Encoding of GnT proteins is performed by genes known as Mgats. Kv3.1b is an alpha subunit of a voltage-gated potassium channel known as Kv3 channels. Kv3 channels have the ability to open and close much more rapidly than other K channels, thus allowing neurons to create trains of action potentials. Kv3.1b is N-glycosylated at two sites, the N220 site and N229. The first aim of this study was to examine caudal primary (CaP) motor neuron development and the motor activity of WT AB larval zebrafish when the N220 site of a Kv3.1b alpha subunit is abolished. The zebrafish expressing N220Q Kv3.1b protein in CaP motor neuron displayed maldeveloped CaP neurons and a significant reduction in motor activity throughout larval development compared to those expressing Wt Kv3.1b protein or EGFP in CaP neurons. The second aim was to determine the effect of atypical N-glycosylation processing in developing zebrafish. Herein, CRISPR/Cas9 was implemented to create the Mgat1b -/-and Mgat1a -/- fish strains for current and future experiments. Mgat1 genes are responsible for the encoding of GnT enzymes. The Mgat1b -/- strain has increased oligomannose type glycans, as demonstrated by the Galanthus Nivalis Lectin (GNL) lectin binding assay. Up until now, the Mgat1b strain has been established, while the Mgat1a strain is still in progress. The locomotor studies indicated that the Mgat1b -/- strain is less active than the WT AB strain. The confocal images suggest cell morphology of CaP neurons are lacking branches. The third and …
author: Hatchett, Cody J
language: en
keywords: glycans, motor neurons, Kv3 channels, neuronal development, motor activity, excitability, cell surface localization, neurodegenerative disorders, spinal cord, GnTI, Mgat1b
date published: 2021-07-29
date modified: 2026-07-24T02:13:39Z
provider: East Carolina University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: East Carolina University

PropertyValue
property ID: Handle
value: http://hdl.handle.net/10342/9382