Diversity of Polyubiquitin Chains

Anirban Adhikari, Zhijian J. Chen

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Polyubiquitin chains linked through different lysines of ubiquitin may exert both proteasome-dependent and -independent functions. In a recent Cell issue, Xu et al. employ quantitative proteomics to profile polyubiquitin linkages in yeast. They find that linkages through all lysines of ubiquitin, except lysine-63, can target proteasomal degradation in vivo, and that lysine-11 polyubiquitination is important for endoplasmic reticulum-associated degradation (ERAD).

Original languageEnglish (US)
Pages (from-to)485-486
Number of pages2
JournalDevelopmental Cell
Volume16
Issue number4
DOIs
StatePublished - Apr 21 2009

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Polyubiquitin
Lysine
Ubiquitin
Endoplasmic Reticulum-Associated Degradation
Degradation
Proteasome Endopeptidase Complex
Proteomics
Yeast
Yeasts

ASJC Scopus subject areas

  • Developmental Biology

Cite this

Diversity of Polyubiquitin Chains. / Adhikari, Anirban; Chen, Zhijian J.

In: Developmental Cell, Vol. 16, No. 4, 21.04.2009, p. 485-486.

Research output: Contribution to journalArticle

Adhikari, Anirban ; Chen, Zhijian J. / Diversity of Polyubiquitin Chains. In: Developmental Cell. 2009 ; Vol. 16, No. 4. pp. 485-486.
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