Ubiquitin dimers control the hydrolase activity of UCH-L3

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• 作者：Rieko Setsuie ; Mikako Sakurai ; Yuriko Sakaguchi ; Keiji Wada
• 关键词：Ubiquitin ; Ubiquitin dimer ; Ubiquitin carboxy terminal hydrolase-L1 (UCH-L1) ; Ubiquitin carboxy terminal hydrolase-L3 (UCH-L3)
• 刊名：Neurochemistry International
• 出版年：2009
• 出版时间：May-June 2009
• 年：2009
• 卷：54
• 期：5-6
• 页码：314-321
• 全文大小：734 K

文摘

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.