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Ubiquitin C-terminal hydrolase L1 (UCH-L1): Structure, distribution and roles in brain function and dysfunction

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)2453-2462
Number of pages10
JournalBiochemical Journal
Volume473
Issue number16
Early online date11 Aug 2016
DOIs
DateAccepted/In press - 6 May 2016
DateE-pub ahead of print - 11 Aug 2016
DatePublished (current) - Aug 2016

Abstract

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 three-dimensional knotted structures yet discovered. Beyond its expression in neurons UCHL1 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.

    Research areas

  • axon, neurites, ubiquitin C-terminal hydrolase L1 (UCH-L1), ubiquitin ligases, ubiquitin proteasome system

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    Rights statement: This is the final published version of the article (version of record). It first appeared online via Portland Press at http://www.biochemj.org/content/473/16/2453.

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