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The regulation of proteasome degradation by multi-ubiquitin chain binding proteins |
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| Authors: | Miller Jayne Gordon Colin |
| Institution: | MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK. |
| Abstract: | The 26S proteasome is a large multi-protein complex that functions to degrade proteins tagged with multi-ubiquitin chains. There are several mechanisms employed by the cell to ensure the efficient delivery of multi-ubiquitinated substrate proteins to the 26S proteasome. This is not only important to ensure the degradation of damaged and misfolded proteins, but also the regulated turnover of critical cell regulators. This discussion will concentrate on what is known about the recognition and delivery of ubiquitinated substrate proteins to the 26S proteasome. |
| Keywords: | 20S CP 20S core particle 19S RP 19S regulatory particle AAA ATPases associated with various cellular activities MHC major histocompatibility complex CSN COP9 signalosome complex UIM ubiquitin interacting motif UBA ubiquitin associated domain UBL ubiquitin like domain VWA Von Willebrand A VCP vasolin containing protein ERAD ER associated degradation UBX ubiquitin regulatory X domain CHIP carboxyl-terminus of Hsc70 Interacting protein VHL Von Hippel-Lindau BAG Bcl2-associated athanogene SCF Skp1-Cul1-Fbox APC/C anaphase promoting complex/cyclosome |
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