Research Mentor(s)

Lina Dahlberg

Affiliated Department

Biology

Sort Order

40

Start Date

15-5-2015 10:00 AM

End Date

15-5-2015 2:00 PM

Keywords

Biology, molecular biology, model organism, C. elegans, glutamate, receptor, protein, mutant, genetics, ubiquitin, endoplasmic reticulum, GLR-1

Document Type

Event

Abstract

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.

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May 15th, 10:00 AM May 15th, 2:00 PM

Regulation of the AMPA glutamate receptor homolog GLR-1 at the endoplasmic reticulum in C. elegans.

Biology

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.

 

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