Abstract 2195 Adapting deGradFP to yeast to study protein degradation

Protein degradation is a fundamental cellular process important for maintaining protein homeostasis and regulating various cellular functions. We are interested in determining how membrane proteins located at different organelles are processed for degradation after they are ubiquitinated. Are they extracted from membranes, packaged into transport vesicles destined for lysosomes, or is an entire organelle degraded? To address this question, we needed a mechanism for ubiquitinating specific proteins on demand.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.110157
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
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article

Abstract 2195 Adapting deGradFP to yeast to study protein degradation

Eric M. Cooper, Chelsea Kotey
Journal of Biological Chemistry
Ubiquitin and proteasome pathways
article

Abstract 2195 Adapting deGradFP to yeast to study protein degradation

Eric M. Cooper, Chelsea Kotey
article en

Abstract

Protein degradation is a fundamental cellular process important for maintaining protein homeostasis and regulating various cellular functions. We are interested in determining how membrane proteins located at different organelles are processed for degradation after they are ubiquitinated. Are they extracted from membranes, packaged into transport vesicles destined for lysosomes, or is an entire organelle degraded? To address this question, we needed a mechanism for ubiquitinating specific proteins on demand.

Journal of Biological ChemistryVol. 301(5)
University School (US), Indiana University School of Medicine, Indiana University (US)
Zero hunger
Openalex Percentile: Top 88%
Ubiquitin and proteasome pathways
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