N-terminal ubiquitination

More protein substrates join in

Aaron Ciechanover, Ronen Ben-Saadon

Research output: Contribution to journalShort surveyResearchpeer-review

260 Citations (Scopus)

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 - 1 Jan 2004

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Ubiquitination
Ubiquitin
Proteins
Polyubiquitin
Proteasome Endopeptidase Complex
Ligases

Cite this

Ciechanover, Aaron ; Ben-Saadon, Ronen. / N-terminal ubiquitination : More protein substrates join in. In: Trends in Cell Biology. 2004 ; Vol. 14, No. 3. pp. 103-106.
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N-terminal ubiquitination : More protein substrates join in. / Ciechanover, Aaron; Ben-Saadon, Ronen.

In: Trends in Cell Biology, Vol. 14, No. 3, 01.01.2004, p. 103-106.

Research output: Contribution to journalShort surveyResearchpeer-review

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