Ubiquitin dimers control the hydrolase activity of UCH-L3.
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.
Mesh Terms:
Animals, Brain, Cell Line, Transformed, Cysteine Endopeptidases, Dimerization, Female, Fibroblasts, Gene Expression Regulation, Enzymologic, Hela Cells, Humans, Hydrolases, Mice, Mice, Transgenic, Ubiquitin, Ubiquitin Thiolesterase, Ubiquitination
Animals, Brain, Cell Line, Transformed, Cysteine Endopeptidases, Dimerization, Female, Fibroblasts, Gene Expression Regulation, Enzymologic, Hela Cells, Humans, Hydrolases, Mice, Mice, Transgenic, Ubiquitin, Ubiquitin Thiolesterase, Ubiquitination
Neurochem. Int.
Date: Jan. 22, 2009
PubMed ID: 19154770
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