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Full-Text Articles in Life Sciences
Transcriptomic Clues To Protein Homeostasis, Anna Byquist, Lina Dahlberg
Transcriptomic Clues To Protein Homeostasis, Anna Byquist, Lina Dahlberg
WWU Honors College Senior Projects
Protein misfolding is associated with many different diseases such as Alzheimer’s disease, Parkinson’s disease, and cystic fibrosis. Cells prevent the accumulation of misfolded proteins through conserved pathways, including Endoplasmic Reticulum Associated Degradation (ERAD). In the absence of proper ERAD function, cellular homeostasis is disrupted, and cells can become stressed. The ERAD mechanism is not fully understood, but it is becoming clear that the intersection of gene regulation and protein degradation are tightly linked (1). We approached this intersection using a strain of C. elegans that is lacking the gene F26F4.9, which encodes a putative ortholog of the mammalian ERAD gene …
Interrogating Centrosome Protein Dynamics, Centriolar Satellite Regulation Mechanisms, And Autofluorescence Characterization Of Caenorhabditis Elegans Using Förster Resonance Energy Transfer-Fluorescence Lifetime Imaging Microscopy (Fret-Flim) And Fluorescence Microscopy, Elizabeth A. Cameron
WWU Graduate School Collection
Centrosomes are required for human cells to divide and differentiate into the many different embryonic tissues that form throughout development. Mutations that drastically disrupt centrosomes cause embryonic lethality and cancer. More subtle mutations cause congenital birth defects including blindness, olfactory deficits, and limb, heart, and brain malformations. PCNT is an essential human gene that encodes for the centrosome protein Pericentrin. Pericentrin organizes the structure of the centrosome by serving as a scaffold protein. Pericentrin also interacts with other centrosome proteins, which play a role in centrosome-mediated microtubule formation. Additionally, Pericentrin recruits enzymes that are involved in centrosome duplication and maturation, …
Roles Of Ubiquitin And Stress In Diacetyl Chemosensation Of C. Elegans, Ellen Zocher, Nelson Ruth, Marissa Hogg
Roles Of Ubiquitin And Stress In Diacetyl Chemosensation Of C. Elegans, Ellen Zocher, Nelson Ruth, Marissa Hogg
Scholars Week
Ubiquitin is a small protein that can be attached to other proteins in a cell, tagging them for destruction. The process of adding ubiquitin to a protein substrate (ubiquitination), and the subsequent trafficking and degradation of this substrate, is a principle regulator of the abundance and activity of many proteins across all forms of life. We are examining the role and dynamics of this regulatory system in the olfactory neurons of the model organism Caenorhabditis elegans, specifically the olfactory receptor protein ODR-10, which allows the worm to detect diacetyl, a volatile compound that is produced by the bacteria the worm …
Regulation Of Ampa-Type Glutamate Receptor Homolog Glr-1 By Erad Ubiquitin Ligases In C. Elegans, Sam Witus
Regulation Of Ampa-Type Glutamate Receptor Homolog Glr-1 By Erad Ubiquitin Ligases In C. Elegans, Sam Witus
Scholars Week
Endoplasmic reticulum-associated degradation (ERAD) maintains cellular health by removing misfolded proteins from the endoplasmic reticulum (ER). ERAD is ubiquitin-dependent, and ubiquitination of target proteins can be catalyzed by ER-resident E3 ubiquitin ligases. In C. elegans, genes for three putative ERAD E3 ubiquitin ligases have been identified: hrd-1, hrdl-1, and marc-6 (HRD-1, GP78/AMFR, and MARCH-6 in mammalian systems). In C. elegans, these three genes cooperate to maintain the overall health of animals during ER stress. We are testing the roles of hrd-1, hrdl-1, and marc-6 in the neurons of C. elegans. GLR-1 is a glutamate receptor that is expressed in a …
Importance Of Ubiquitin-Mediated Degradation On Diacetyl Chemosensation In C. Elegans, Ellen Zocher, Nelson Ruth
Importance Of Ubiquitin-Mediated Degradation On Diacetyl Chemosensation In C. Elegans, Ellen Zocher, Nelson Ruth
Scholars Week
Ubiquitin is a small regulatory protein that can be attached to other proteins in a cell, tagging them for destruction. Ubiquitin plays a critical role in regulating the abundance and activity of many proteins. We examined the role of ubiquitin and the cellular pathway it follows in olfactory neurons in the model organism C. elegans. C. elegans senses and moves towards sources of diacetyl, a volatile compound generated by the bacteria it consumes. This behavior is dependent on the diacetyl receptor, ODR-10. We hypothesized that the ubiquitin-mediated degradation system is involved in the regulation of this sensory receptor. Using transgenic …