TY - JOUR
T1 - RING-type E3 ligases
T2 - Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
AU - Metzger, Meredith B.
AU - Pruneda, Jonathan N.
AU - Klevit, Rachel E.
AU - Weissman, Allan M.
N1 - Funding Information:
The study of RING-type E3s continues to grow extremely rapidly. We regret that it was possible to only cite a fraction of the outstanding primary publications in this field. This work was supported by the National Institute of General Medical Sciences grants R01 GM088055 and R01 GM098503 (R.E.K.) and by the Intramural Research Program of the National Institutes of Health, National Cancer Institute, Center for Cancer Research (A.M.W.).
PY - 2014/1
Y1 - 2014/1
N2 - RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
AB - RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
KW - Catalysis
KW - Protein degradation
KW - RING finger
KW - U-box
KW - Ubiquitin ligase (E3)
KW - Ubiquitin-conjugating enzyme (E2)
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U2 - 10.1016/j.bbamcr.2013.05.026
DO - 10.1016/j.bbamcr.2013.05.026
M3 - Review article
AN - SCOPUS:84890176335
SN - 0167-4889
VL - 1843
SP - 47
EP - 60
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
IS - 1
ER -