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Publication - Professor Jeremy Henley

    Ubiquitin C-terminal hydrolase L1 (UCH-L1)

    Structure, distribution and roles in brain function and dysfunction

    Citation

    Bishop, P, Rocca, D & Henley, J, 2016, ‘Ubiquitin C-terminal hydrolase L1 (UCH-L1): Structure, distribution and roles in brain function and dysfunction’. Biochemical Journal, vol 473., pp. 2453-2462

    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.

    Full details in the University publications repository