Description
Title: Control of Yeast Protein Quality Using Nuclear-Cytoplasmic Localization and Ubiquitin Ligase Redundancy
Abstract: Proteins’ various functions all rely on proper three-dimensional folding and assembly. Misfolded cellular proteins may cause damage to cells by aggregating in their resident compartments and interfering with essential cellular functions or securing crucial components. These abnormal proteins are repaired or eliminated by protein quality control (PQC) pathways. Most frequently, the ubiquitin-proteasome system (UPS) is used to identify and destroy proteins that molecular chaperones are unable to refold. A subset of ubiquitin ligases (also known as E3s) that function in various cellular compartments ubiquitylate misfolded substrates. The most prominent ligases mediating cytoplasmic and nuclear PQC have overlapping yet different substrate specificities, according to recent research in Saccharomyces cerevisiae. According to their location, many different ubiquitin ligases can target different substrates, and cytoplasmic PQC substrates can be directed to the nucleus for ubiquitylation and degradation. In this article, we’ll go over some of the most important yeast PQC ubiquitin ligases that are active in the cytoplasm and nucleus, as well as the most recent data showing how these ligases frequently work redundantly toward substrates in these compartments.
Keywords: protein degradation; proteasome; ubiquitin; degron; protein quality control; ubiquitin ligase
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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