期刊
BIOCHEMICAL JOURNAL
卷 473, 期 -, 页码 2453-2462出版社
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20160082
关键词
axon; neurites; ubiquitin C-terminal hydrolase L1 (UCH-L1); ubiquitin ligases; ubiquitin proteasome system
资金
- Alzheimer's Society [ALZSOC-2012-002]
- Biotechnology and Biological Sciences Research Council [PG/14/60/31014]
- British Heart Foundation [PG/14/60/31014]
- European Research Council [232881]
- Medical Research Council [MR/L003791/1]
- BBSRC [BB/K014366/1, BB/K014358/1] Funding Source: UKRI
- MRC [MR/L003791/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K014366/1, BB/K014358/1] Funding Source: researchfish
- Medical Research Council [MR/L003791/1] Funding Source: researchfish
- European Research Council (ERC) [232881] Funding Source: European Research Council (ERC)
Ubiquitin C-terminal hydrolase L1 (UCH-L1) is an extremely abundant protein in the brain where, remarkably, it is estimated to make up 1-5% of total neuronal protein. Although it comprises only 223 amino acids it has one of the most complicated 3D knotted structures yet discovered. Beyond its expression in neurons UCH-L1 has only very limited expression in other healthy tissues but it is highly expressed in several forms of cancer. Although UCH-L1 is classed as a deubiquitinating enzyme (DUB) the direct functions of UCH-L1 remain enigmatic and a wide array of alternative functions has been proposed. UCH-L1 is not essential for neuronal development but it is absolutely required for the maintenance of axonal integrity and UCH-L1 dysfunction is implicated in neurodegenerative disease. Here we review the properties of UCH-L1, and how understanding its complex structure can provide new insights into its roles in neuronal function and pathology.
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