Degradation of proteins
From WikiLectures
In eukaryotic cells, there are two main ways in which proteins are broken down into peptide residues:
- Autophagy (from the Greek for "self-eating"), which removes long-lived proteins or larger structures such as organelles, by transporting them to the lysosome, where they are cleaved[1].
- Proteins that have a shorter lifespan, which is the vast majority (about 90%) of all degraded proteins, are not degraded in a membrane organelle such as a lysosome, but freely in the cytosol or in the nucleus by a multiprotein complex called the proteasome.
More detailed information on protein degradation can be found on the following pages:
- Physiology
- Lysosomes
- Proteasomes (general basis)
- Degradation of proteins on proteasomes
- Pathology
Links[edit | edit source]
Related articles[edit | edit source]
- Proteins
- Ubiquitination
- Deubiquitination
- History of the ubiquitin-proteasome system
- Proteasome inhibitors
- Proteasome (in detail)
Source[edit | edit source]
- CVEK, Boris. Od ubikvitinu k antabusu. Britské listy : deník o všem, o čem se v České republice příliš nemluví [online]. 2011, vol. -, p. -, Available from <https://blisty.cz//legacy.blisty.cz/art/56680.html>. ISSN 1213-1792.
Reference[edit | edit source]
- ↑ TODDE, Virginia – VEENHUIS, Marten – VAN DER KLEI, Ida J. Autophagy: principles and significance in health and disease. Biochim Biophys Acta [online]. 2009, y. 1792, p. 3-13, Available from <https://www.ncbi.nlm.nih.gov/pubmed/19022377>. ISSN 0006-3002.
