Abstract：
:Ubiquitin (Ub) carboxy terminal hydrolase (UCH)-L1 and UCH-L3 are two of the deubiquitinating enzymes expressed in the brain. Both gad mice, which lack UCH-L1 expression and Uchl3 knockout mice exhibit neurodegeneration, although at distinct areas. These phenotypes indicate the importance of UCH-L1 and UCH-L3 in the regulation of the central nervous system. However, molecular substrates and the molecular regulators of UCH-L1 and UCH-L3 remain poorly identified. Here we show that Ub dimers interact non-covalently with UCH-L3 in vitro and in cells. These interactions were not observed with UCH-L1 in cells. In vitro, K48-linked Ub dimers pronouncedly inhibited the hydrolase activity of UCH-L3, while mono-Ub, a previously identified interacting protein, inhibited the hydrolase activity of UCH-L1. These results indicate that mono-Ub and Ub dimers may regulate the enzymatic functions of UCH-L1 and UCH-L3, respectively, in vivo.
journal_name
Neurochem Intjournal_title
Neurochemistry internationalauthors
Setsuie R,Sakurai M,Sakaguchi Y,Wada Kdoi
10.1016/j.neuint.2008.12.013subject
Has Abstractpub_date
2009-05-01 00:00:00pages
314-21issue
5-6eissn
0197-0186issn
1872-9754pii
S0197-0186(08)00215-5journal_volume
54pub_type
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