No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription.
The ubiquitin-proteasome pathway (UPP) is responsible for most programmed turnover of proteins in eukaryotic cells, and this activity has been known for some time to be involved in transcriptional regulation. More recently, intersections of the UPP and transcription have been discovered that are not proteolytic in nature and appear to revolve around the chaperonin-like activities of the ATPases in the 19 S regulatory subunit of the proteasome. Moreover, monoubiquitylation, which does not signal degradation, has been found to be a key modification of many transcription factors and histones. These various non-proteolytic roles of the UPP in transcription are reviewed here, and plausible mechanistic models are discussed.
Kodadek
Thomas
T
Department of Chemistry, The Scripps Research Institute, Scripps Florida, Jupiter, Florida 33458, USA. kodadek@scripps.edu
D000818:Animals; D005057:Eukaryotic Cells / Q000502:physiology*; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D012326:RNA Splicing / Q000502:physiology*; D014158:Transcription, Genetic / Q000502:physiology*; D025801:Ubiquitin / Q000502:physiology*
D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex