Investigating the effects of glutamate trafficking and receptor mutations on the unfolded protein response (UPR) in C. elegans
Senior Project Advisor
Dahlberg, Lina
Document Type
Project
Publication Date
Spring 2020
Keywords
Glutamate, nmr-1, glr-1, eat-4, hsp-4, ire-1, xbp-1, xbp-1s, hsp4p::gfp, ak4, zcIs4, ER, endoplasmic reticulum, ER stress, UPR, Unfolded protein response, tunicamycin, neuron, neurotransmitter, non-cell autonomous signaling, C. elegans
Abstract
The endoplasmic reticulum (ER) is responsible for properly folding and transporting proteins. Protein misfolding may cause excess stress on the ER by which some genetic mutations as well as environmental triggers can cause stress in the ER which can lead to an accumulation of misfolded proteins, which can lead to cell death. Additionally, neuronal signaling dysfunction has been implicated in Alzheimer’s, Parkinson’s, and various neurodegenerative disorders.
Taylor et. al 2011 has shown UPR non-cell autonomous signaling from neurons to intestinal cells; however, the area of glutamate signaling was not explored. Here I investigate this by performing ER stress assays using an ER stressing molecule, tunicamycin, on the model organism C. elegans carrying a non-functional glutamate receptor (nmr-1) a reporter construct (hsp-4p::gfp). The animals were subjected to these assays and qualitatively analyzed for UPR activation via microscopy imaging, followed by quantitative analysis via Western blotting technique. The data indicate that the nmr-1 mutant animals are sensitized to ER stress which results in increased UPR, which complements the Taylor et. al 2011 study. Data collected from this study merits further investigation of other genes involved in glutamate signaling such as glr-1 and eat-4 to fully understand glutamate signaling on the UPR.
Department
Biology
Recommended Citation
Takasaki, Savanna, "Investigating the effects of glutamate trafficking and receptor mutations on the unfolded protein response (UPR) in C. elegans" (2020). WWU Honors College Senior Projects. 390.
https://cedar.wwu.edu/wwu_honors/390
Subjects - Topical (LCSH)
Glutamic acid; Endoplasmic reticulum--Pathophysiology; Protein folding; Cellular signal transduction; Genetic translation; Nematodes
Genre/Form
student projects; term papers
Type
Text
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 document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.
Language
English
Format
application/pdf