Premium
The regulation of proteasome degradation by multi‐ubiquitin chain binding proteins
Author(s) -
Miller Jayne,
Gordon Colin
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.042
Subject(s) - proteasome , ubiquitin , microbiology and biotechnology , protein degradation , degradation (telecommunications) , chemistry , ubiquitin protein ligases , ubiquitin conjugating enzyme , substrate (aquarium) , ubiquitin ligase , biochemistry , biology , computer science , gene , telecommunications , ecology
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.