Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1995-01

AUTHORS

Martin Scheffner, Ulrike Nuber, Jon M. Huibregtse

ABSTRACT

UBIQUITINATION of proteins involves the concerted action of the El ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzymes and E3 ubiquitin–protein 1igases1–3. It has been proposed that E3s function as 'docking proteins', specifically binding substrate proteins and specific E2s, and that ubiquitin is then transferred directly from E2s to substrates1–5. We show here that formation of a ubiquitin thioester on E6–AP, an E3 involved in the human papillomavirus E6-induced ubiquitination of p53 (refs 6–10), is an intermediate step in E6-AP-dependent ubiquitination. The order of ubiquitin transfer is from El to E2, from E2 to E6-AP, and finally from E6-AP to a substrate. This cascade of ubiquitin thioester complexes suggests that E3s have a defined enzymatic activity and do not function simply as docking proteins. The cysteine residue of E6-AP responsible for ubiquitin thioester formation was mapped to a region that is highly conserved among several proteins of unknown function, suggesting that these proteins share the ability to form thioesters with ubiquitin. More... »

PAGES

81-83

Journal

TITLE

Nature

ISSUE

6509

VOLUME

373

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/373081a0

    DOI

    http://dx.doi.org/10.1038/373081a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1014213505

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7800044


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