Protein Quality Control in the Nucleus
Autor: | Caio A. Rebula, Esben G. Poulsen, Sofie V. Nielsen, Rasmus Hartmann-Petersen |
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Jazyk: | angličtina |
Rok vydání: | 2014 |
Předmět: |
Protein Folding
Active Transport Cell Nucleus SUMO protein lcsh:QR1-502 Review Biochemistry lcsh:Microbiology stress JUNQ and IPOD ubiquitin Protein biosynthesis Animals Humans chaperone Nuclear protein Molecular Biology degradation Cell Nucleus biology Nuclear Proteins misfolding Cell biology Aggresome proteasome Proteasome SUMO Chaperone (protein) biology.protein Protein folding |
Zdroj: | Biomolecules, Vol 4, Iss 3, Pp 646-661 (2014) Nielsen, S V, Poulsen, E G, Rebula, C A & Hartmann-Petersen, R 2014, ' Protein quality control in the nucleus ', Biomolecules, vol. 4, no. 3, pp. 646-661 . https://doi.org/10.3390/biom4030646 Biomolecules |
Popis: | In their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. Since such partially denatured proteins are prone to aggregate, cells have evolved several elaborate quality control systems to deal with these potentially toxic proteins. First, various molecular chaperones will seize the misfolded protein and either attempt to refold the protein or target it for degradation via the ubiquitin-proteasome system. The degradation of misfolded proteins is clearly compartmentalized, so unique degradation pathways exist for misfolded proteins depending on whether their subcellular localization is ER/secretory, mitochondrial, cytosolic or nuclear. Recent studies, mainly in yeast, have shown that the nucleus appears to be particularly active in protein quality control. Thus, specific ubiquitin-protein ligases located in the nucleus, target not only misfolded nuclear proteins, but also various misfolded cytosolic proteins which are transported to the nucleus prior to their degradation. In comparison, much less is known about these mechanisms in mammalian cells. Here we highlight recent advances in our understanding of nuclear protein quality control, in particular regarding substrate recognition and proteasomal degradation. |
Databáze: | OpenAIRE |
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