Ubiquitin family proteins and their relationship to the proteasome: a structural perspective |
| |
Authors: | Walters Kylie J Goh Amanda M Wang Qinghua Wagner Gerhard Howley Peter M |
| |
Institution: | Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA. |
| |
Abstract: | Many biological processes rely on targeted protein degradation, the dysregulation of which contributes to the pathogenesis of various diseases. Ubiquitin plays a well-established role in this process, in which the covalent attachment of polyubiquitin chains to protein substrates culminates in their degradation via the proteasome. The three-dimensional structural topology of ubiquitin is highly conserved as a domain found in a variety of proteins of diverse biological function. Some of these so-called "ubiquitin family proteins" have recently been shown to bind components of the 26S proteasome via their ubiquitin-like domains, thus implicating proteasome activity in pathways other than protein degradation. In this chapter, we provide a structural perspective of how the ubiquitin family of proteins interacts with the proteasome. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|