20S proteasome biogenesis |
| |
Authors: | Krüger E Kloetzel P M Enenkel C |
| |
Affiliation: | 1. Department of Biochemistry, Faculty of Science, The M.S. University of Baroda, Vadodara 390 002, Gujarat, India;2. Spinal Cord and Brain Injury Research Center, Department of Pathology and Laboratory Medicine, University of Kentucky, 800 S. Limestone, Lexington, KY 40536, USA;3. Neuroscience, University of Kentucky, Lexington, KY 40536, USA;4. Department of Cell and Developmental Biology, University College London, Gower Street, London WC1E 6BT, UK |
| |
Abstract: | 26S proteasomes are multi-subunit protease complexes responsible for the turnover of short-lived proteins. Proteasomal degradation starts with the autocatalytic maturation of the 20S core particle. Here, we summarize different models of proteasome assembly. 20S proteasomes are assembled as precursor complexes containing alpha and unprocessed beta subunits. The propeptides of the beta subunits are thought to prevent premature conversion of the precursor complexes into matured particles and are needed for efficient beta subunit incorporation. The complex biogenesis is tightly regulated which requires additional components such as the maturation factor Ump1/POMP, an ubiquitous protein in eukaryotic cells. Ump1/POMP is associated with precursor intermediates and degraded upon final maturation. Mammalian proteasomes are localized all over the cell, while yeast proteasomes mainly localize to the nuclear envelope/endoplasmic reticulum (ER) membrane network. The major localization of yeast proteasomes may point to the subcellular place of proteasome biogenesis. |
| |
Keywords: | |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|