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- W2007588515 endingPage "28" @default.
- W2007588515 startingPage "17" @default.
- W2007588515 abstract "Post-translational modification of proteins with ubiquitin regulates a variety of eukaryotic cellular processes. Ubiquitin can be conjugated to substrates either as a single moiety (monoubiquitination) or as isopeptide bond-linked chains (polyubiquitination), creating an array of ubiquitin signals. It has been established that monoubiquitination can serve important functions in many biological processes such as the regulation of gene transcription, protein trafficking, and DNA repair. Surprisingly, little is known about the mechanisms by which monoubiquitin signals are produced in the cell. Here, we discuss the potential cellular strategies for generating monoubiquitinated proteins using a few, relatively well characterized examples of monoubiquitinated proteins. These strategies include coupling ubiquitination to low affinity ubiquitin binding, using monoubiquitination-dedicated E2 conjugating enzymes, and restricting ubiquitin chain elongation. Some of these principles may be applicable to protein modifications involving ubiquitin like proteins (UBLs), which often occur in monomeric form." @default.
- W2007588515 created "2016-06-24" @default.
- W2007588515 creator A5046551911 @default.
- W2007588515 creator A5073033280 @default.
- W2007588515 date "2011-10-08" @default.
- W2007588515 modified "2023-09-26" @default.
- W2007588515 title "Cellular strategies for making monoubiquitin signals" @default.
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