期刊
CELL DEATH AND DIFFERENTIATION
卷 28, 期 2, 页码 455-472出版社
SPRINGERNATURE
DOI: 10.1038/s41418-020-00707-6
关键词
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资金
- National Health & Medical Research Council (NHMRC) [1158366]
- NHMRC Senior Principal Research Fellowship [1103006]
- University of South Australia
- National Health and Medical Research Council of Australia [1158366, 1103006] Funding Source: NHMRC
HECT E3s form a small family of highly conserved enzymes that regulate key signaling pathways by accepting ubiquitin from E2 ubiquitin conjugating enzymes. The activity and functional regulation of these enzymes are controlled by several factors including post-translational modifications, inter- and intramolecular interactions, and binding of co-activators and adaptor proteins.
The HECT (homologous to E6AP C-terminus) ubiquitin ligases (E3s) are a small family of highly conserved enzymes involved in diverse cellular functions and pathological conditions. Characterised by a C-terminal HECT domain that accepts ubiquitin from E2 ubiquitin conjugating enzymes, these E3s regulate key signalling pathways. The activity and functional regulation of HECT E3s are controlled by several factors including post-translational modifications, inter- and intramolecular interactions and binding of co-activators and adaptor proteins. In this review, we focus on the regulation of HECT E3s by accessory proteins or adaptors and discuss various ways by which adaptors mediate their regulatory roles to affect physiological outcomes. We discuss common features that are conserved from yeast to mammals, regardless of the type of E3s as well as shed light on recent discoveries explaining some existing enigmas in the field.
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