Diversity of Polyubiquitin Chains

Anirban Adhikari; Zhijian J. Chen

doi:10.1016/j.devcel.2009.04.001

Diversity of Polyubiquitin Chains

Anirban Adhikari, Zhijian J. Chen

Research output: Contribution to journal › Short survey › peer-review

57 Scopus citations

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 language	English (US)
Pages (from-to)	485-486
Number of pages	2
Journal	Developmental cell
Volume	16
Issue number	4
DOIs	https://doi.org/10.1016/j.devcel.2009.04.001
State	Published - Apr 21 2009

ASJC Scopus subject areas

Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Developmental Biology
Cell Biology

Access to Document

10.1016/j.devcel.2009.04.001

Cite this

@article{27e4245d8f6d4b12b62b548ceac6d0a4,

title = "Diversity of Polyubiquitin Chains",

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).",

author = "Anirban Adhikari and Chen, {Zhijian J.}",

year = "2009",

month = apr,

day = "21",

doi = "10.1016/j.devcel.2009.04.001",

language = "English (US)",

volume = "16",

pages = "485--486",

journal = "Developmental cell",

issn = "1534-5807",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - Diversity of Polyubiquitin Chains

AU - Adhikari, Anirban

AU - Chen, Zhijian J.

PY - 2009/4/21

Y1 - 2009/4/21

N2 - 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).

AB - 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).

UR - http://www.scopus.com/inward/record.url?scp=64549154396&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=64549154396&partnerID=8YFLogxK

U2 - 10.1016/j.devcel.2009.04.001

DO - 10.1016/j.devcel.2009.04.001

M3 - Short survey

C2 - 19386255

AN - SCOPUS:64549154396

SN - 1534-5807

VL - 16

SP - 485

EP - 486

JO - Developmental cell

JF - Developmental cell

IS - 4

ER -

Diversity of Polyubiquitin Chains

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this