Premium
Proteasome plasticity
Author(s) -
Glickman Michael H.,
Raveh Dina
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.2005.04.048
Subject(s) - proteasome , proteolysis , ubiquitin , microbiology and biotechnology , importin , intracellular , function (biology) , ribosome , biology , biochemistry , chemistry , enzyme , cell nucleus , nuclear transport , rna , nucleus , gene
The 26S proteasome is responsible for regulated proteolysis of most intracellular proteins yet the focus of intense regulatory action itself. Proteasome abundance is responsive to cell needs or stress conditions, and dynamically localized to concentrations of substrates. Proteasomes are continually assembled and disassembled, and their subunits subject to a variety of posttranslational modifications. Furthermore, as robust and multi‐tasking as this complex is, it does not function alone. A spattering of closely associating proteins enhances complex stability, fine‐tunes activity, assists in substrate‐binding, recycling of ubiquitin, and more. HEAT repeat caps activate proteasomes, yet share remarkable features with nuclear importins. Fascinating cross talk even occurs with ribosomes through common maturation factors. The dynamics of proteasome configurations and how they relate to diverse activities is the topic of this review.