Ub on the move

Natalia Shcherbik, Dale S. Haines

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Ubiquitination is an increasingly common post-translation modification that controls both the expression and activity of numerous proteins in the eukaryotic cell. One frequent target of the ubiquitin (Ub) modification machinery is transcription factors. Although ubiquitination generally modulates their function by inducing proteasome-dependent degradation, past and recent studies indicate that ubiquitination also regulates nuclear-cytoplasmic trafficking of transcriptional regulators. Ubiquitination is known to modulate transcription factor localization by destroying sequestering proteins and by directly promoting nuclear import and export of modified substrates. This review discusses old and new paradigms relating Ub modification and the control of transcription factor shuttling in and out of the nucleus.

Original languageEnglish (US)
Pages (from-to)11-19
Number of pages9
JournalJournal of Cellular Biochemistry
Volume93
Issue number1
DOIs
StatePublished - Dec 1 2004

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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