N-terminal ubiquitination: More protein substrates join in

Aaron Ciechanover, Ronen Ben-Saadon

Research output: Contribution to journalShort surveypeer-review

307 Scopus citations

Abstract

The ubiquitin-proteasome system (UPS) is involved in selective targeting of innumerable cellular proteins through a complex pathway that plays important roles in a broad array of processes. An important step in the proteolytic cascade is specific recognition of the substrate by one of many ubiquitin ligases, E3s, which is followed by generation of the polyubiquitin degradation signal. For most substrates, it is believed that the first ubiquitin moiety is conjugated, through its C-terminal Gly76 residue, to an ε-NH2 group of an internal Lys residue. Recent findings indicate that, for several proteins, the first ubiquitin moiety is fused linearly to the α-NH 2 group of the N-terminal residue. An important biological question relates to the evolutionary requirement for an alternative mode of ubiquitination.

Original languageEnglish
Pages (from-to)103-106
Number of pages4
JournalTrends in Cell Biology
Volume14
Issue number3
DOIs
StatePublished - Mar 2004

ASJC Scopus subject areas

  • Cell Biology

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