Research Mentor(s)
Dahlberg, Lina
Description
In C. elegans, the glutamate receptor GLR-1 functions in the nervous system to decode environmental stimuli and sensory experiences, and to regulate locomotion and the formation of long-term memory. C. elegans GLR-1 is homologous to mammalian glutamate receptors, and we can use this simple organism as a system to better understand the life cycle of human receptors (1). Because GLR-1 is a membrane protein, it is first assembled in the interior of a neuron, and then it is transported to the membrane at the surface of the cell so that it can receive chemical signals (glutamate) from the environment. Currently, many of the detailed cellular mechanisms that regulate the abundance of GLR-1 after it has been exported to the cell surface are known (2, 3). However, it is less clear how the abundance of GLR-1 is regulated in the interior of the cell prior to being transported to the cell surface. Before GLR-1 is exported to the cell surface it must be properly folded into its active conformation at the endoplasmic reticulum (ER). Here we investigate the role of three E3-ubiquitin ligases that function in endoplasmic reticulum associated degradation (ERAD) HRD-1, HRDL-1, and MARC-6. Using fluorescence microscopy HRDL-1 depleted C. elegans display wide patches of GLR-1::GFP suggesting accumulation of the protein at the ER. We also employ Western blotting to determine the relative concentrations of GLR-1 in the absence of E3-ubiquitin ligases. Our research suggests that the depletion of HRDL-1 causes accumulation of GLR-1.
Document Type
Event
Start Date
15-5-2015 10:00 AM
End Date
15-5-2015 2:00 PM
Department
Biology
Genre/Form
student projects; posters
Subjects – Topical (LCSH)
Caenorhabditis elegans--Genetics; Cell receptors
Type
Image
Keywords
Biology, molecular biology, model organism, C. elegans, glutamate, receptor, protein, mutant, genetics, ubiquitin, endoplasmic reticulum, GLR-1
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this documentation for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.
Language
English
Format
application/pdf
Included in
Regulation of the AMPA glutamate receptor homolog GLR-1 at the endoplasmic reticulum in C. elegans.
In C. elegans, the glutamate receptor GLR-1 functions in the nervous system to decode environmental stimuli and sensory experiences, and to regulate locomotion and the formation of long-term memory. C. elegans GLR-1 is homologous to mammalian glutamate receptors, and we can use this simple organism as a system to better understand the life cycle of human receptors (1). Because GLR-1 is a membrane protein, it is first assembled in the interior of a neuron, and then it is transported to the membrane at the surface of the cell so that it can receive chemical signals (glutamate) from the environment. Currently, many of the detailed cellular mechanisms that regulate the abundance of GLR-1 after it has been exported to the cell surface are known (2, 3). However, it is less clear how the abundance of GLR-1 is regulated in the interior of the cell prior to being transported to the cell surface. Before GLR-1 is exported to the cell surface it must be properly folded into its active conformation at the endoplasmic reticulum (ER). Here we investigate the role of three E3-ubiquitin ligases that function in endoplasmic reticulum associated degradation (ERAD) HRD-1, HRDL-1, and MARC-6. Using fluorescence microscopy HRDL-1 depleted C. elegans display wide patches of GLR-1::GFP suggesting accumulation of the protein at the ER. We also employ Western blotting to determine the relative concentrations of GLR-1 in the absence of E3-ubiquitin ligases. Our research suggests that the depletion of HRDL-1 causes accumulation of GLR-1.