Article
N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system.
Journal of proteomics - 1 Jan 2016
Kimura Ayuko, Kurata Yoichi, Nakabayashi Jun, Kagawa Hiroyuki, Hirano Hisashi
Abstract excerpt
Ubiquitination is the posttranslational modification of a protein by covalent attachment of ubiquitin. Controlled proteolysis via the ubiquitin-proteasome system (\UPS) alleviates cellular stress by clearing misfolded proteins. In budding yeast, UPS within the nucleus degrades the nuclear proteins as well as proteins imported from the cytoplasm. While the predominantly nuclear localization of the yeast proteasome...
Topics
- Adenosine Triphosphatases
- Cell Nucleus
- Cytoplasm
- Endoplasmic Reticulum
- Gene Expression Regulation, Fungal
- HSP70 Heat-Shock Proteins
- Mass Spectrometry
- Molecular Chaperones
- Mutation
- Myristic Acid
- Proteasome Endopeptidase Complex
- Protein Folding