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Analyzing The Effect Of Apoptotic Mutations On The State Of The Nascent-Polypeptide Associated Complex In Caenorhabditis Elegans, Monica Gerber
Analyzing The Effect Of Apoptotic Mutations On The State Of The Nascent-Polypeptide Associated Complex In Caenorhabditis Elegans, Monica Gerber
Senior Honors Projects, 2010-2019
Cells experiencing misfolded protein stress can become debilitated and die, contributing to the onset of disease. The nascent polypeptide-associated complex (NAC) is a heterodimeric translational chaperone that protects against misfolded protein stress by mediating proper protein folding and localization during translation. Depletion of this complex results in misfolded protein accumulation in the endoplasmic reticulum (ER). To determine the importance of the NAC to proteostasis, we have previously depleted the complex in C.elegans via RNA interference and observed numerous dose-dependent effects, including apoptosis of neuronal cells and changes in gene expression of hypodermal cells. While we have observed these cell-specific responses …
The Fate Of Icd-1 During Misfolded Protein Induced Apoptosis In Caenorhabditis Elegans, Kyle H. Perez
The Fate Of Icd-1 During Misfolded Protein Induced Apoptosis In Caenorhabditis Elegans, Kyle H. Perez
Senior Honors Projects, 2010-2019
Severe misfolded protein stress initiates cellular responses that often result in the death of the affected cell, typically by apoptosis. An essential aspect of apoptosis is caspase-mediated cleavage of proteins that, once cleaved, further propagate death. One heterodimeric structure putatively targeted in this process in the nascent polypeptide-associated complex (NAC), a translational chaperone thought to help prevent misfolded protein stress in the ER. The purpose of this investigation was to determine whether the beta subunit of the NAC in C. elegans (ICD-1) is cleaved during the induction of apoptosis, with the hypothesis that ICD-1 is cleaved during stressed-induced apoptosis to …
Profile Of The Unfolded Protein Response In C. Elegans Depleted Of The Translational Chaperone, Nac., Caylin S. Murray
Profile Of The Unfolded Protein Response In C. Elegans Depleted Of The Translational Chaperone, Nac., Caylin S. Murray
Masters Theses, 2010-2019
The function of a protein is a direct consequence of its final structure, which is achieved by protein-folding processes that generate a tertiary state through the juxtaposition of locally formed secondary structures. Because all cells need functional proteins to survive, each contains robust and redundant mechanisms that regulate the folding of newly forming proteins, and the refolding of misfolded proteins that are often generated during stress. Essential to these mechanisms, chaperones are proteins that aid in protein folding of nascent and misfolding protein without being incorporated in the final structure. One chaperone complex, the nascent polypeptide-associated complex (NAC), aids in …
The Role Of The Nascent Polypeptide-Associated Complex In Caenorhabditis Elegans, Paul T. Arsenovic
The Role Of The Nascent Polypeptide-Associated Complex In Caenorhabditis Elegans, Paul T. Arsenovic
Masters Theses, 2010-2019
The nascent polypeptide-associated complex (NAC) is a highly conserved protein complex known to play an important role in the development of metazoan organisms, but its molecular function is not well understood. Recent evidence from experiments using Saccharomyces cerevisiae as model supported the hypothesis that the NAC is either a chaperone or a component of the cytosolic chaperone network that interacts with nascent peptides emerging from the ribosome. We tested this model in C. elegans and found that the homologues of the NAC , icd-1 and icd-2, behave like chaperones in the worm. Lack of icd-1 or icd-2 altered the worms …