Event Title

Effects of ERAD E3 ligase mutations on C. elegans food seeking behavior

Research Mentor(s)

Lina Dahlberg

Description

Endoplasmic Reticulum Associated Degradation (ERAD) is a cellular process that prevents protein aggregation by tagging misfolded proteins with ubiquitin at the endoplasmic reticulum (ER), marking them for destruction (figure 1) (7,6,5). E3 ubiquitin ligases participate in the ubiquination process of target proteins during ERAD (figure 1) (7,6,5). Protein aggregation is important to study because it is seen in neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease (7). In order to research how ERAD works to prevent protein aggregation, a model protein, GLR-1, is used for this research. GLR-1 is required for food seeking behaviors in the microscopic worm, C. elegans (3). In order to understand what interactions GLR-1 may have with each of the E3 ligases that are involved in the ERAD pathway, the food seeking behavior of three different C. elegans strains that each have one mutated, non-functional E3 ligase, hrdl-1, hrd-1 and marc-6, were tested and compared.

Document Type

Event

Start Date

17-5-2018 9:00 AM

End Date

17-5-2018 12:00 PM

Location

Biology

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

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May 17th, 9:00 AM May 17th, 12:00 PM

Effects of ERAD E3 ligase mutations on C. elegans food seeking behavior

Biology

Endoplasmic Reticulum Associated Degradation (ERAD) is a cellular process that prevents protein aggregation by tagging misfolded proteins with ubiquitin at the endoplasmic reticulum (ER), marking them for destruction (figure 1) (7,6,5). E3 ubiquitin ligases participate in the ubiquination process of target proteins during ERAD (figure 1) (7,6,5). Protein aggregation is important to study because it is seen in neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease (7). In order to research how ERAD works to prevent protein aggregation, a model protein, GLR-1, is used for this research. GLR-1 is required for food seeking behaviors in the microscopic worm, C. elegans (3). In order to understand what interactions GLR-1 may have with each of the E3 ligases that are involved in the ERAD pathway, the food seeking behavior of three different C. elegans strains that each have one mutated, non-functional E3 ligase, hrdl-1, hrd-1 and marc-6, were tested and compared.