Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1843, Issue 1, Pages 47-60Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2013.05.026
Keywords
RING finger; U-box; Ubiquitin ligase (E3); Ubiquitin-conjugating enzyme (E2); Protein degradation; Catalysis
Categories
Funding
- National Institute of General Medical Sciences [R01 GM088055, R01 GM098503]
- National Institutes of Health, National Cancer Institute, Center for Cancer Research
- NATIONAL CANCER INSTITUTE [ZIABC009392, ZIABC010292] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM098503, R01GM088055] Funding Source: NIH RePORTER
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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. Published by Elsevier B.V.
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