title: Ubiquitination of newly synthesized proteins at the ribosome.
abstract: Newly synthesized proteins can be misfolded or damaged because of errors during synthesis or environmental insults (e.g., heat shock), placing a significant burden on protein quality control systems. In addition, numerous human diseases are associated with a deficiency in eliminating aberrant proteins or accumulation of aggregated proteins. Understanding the mechanisms of protein quality control and disposal pathways for misfolded proteins is therefore crucial for therapeutic intervention in these diseases. Quality control processes function at many points in the life cycle of proteins, and a subset act at the actual site of protein synthesis, the ribosome. Here we summarize recent advances in the role of the ubiquitin proteasome system in protein quality control during the process of translation.
authors.affiliation: Department of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Feng
authors.initials: F
authors.lastname: Wang
authors.affiliation: Department of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Larissa A
authors.initials: LA
authors.lastname: Canadeo
authors.affiliation: Department of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: huibregtse@austin.utexas.edu.
authors.forename: Jon M
authors.initials: JM
authors.lastname: Huibregtse
mesh_terms: D000818:Animals; D006801:Humans; D014176:Protein Biosynthesis; D017510:Protein Folding; D012270:Ribosomes / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000502:physiology; D054875:Ubiquitination
chemical_list: D044767:Ubiquitin-Protein Ligases
keywords: Co-translational ubiquitination; Ltn1; Protein quality control; Ribosome; Ubiquitin