Cloning and Characterization of DULP, a Novel Ubiquitin-Like Molecule from Human Dendritic Cells
Cloning and Characterization of DULP, a Novel Ubiquitin-Like Molecule from Human Dendritic Cells
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DULP(一种来自人类树突状细胞的新型泛素样分子)的克隆和表征
DOI:
10.1038/cmi.2009.4
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发表时间:
2009-02-01
影响因子:
24.1
通讯作者:
Yu, Yizhi
中科院分区:
文献类型:
--
作者:
Liu, Guoyan;Liu, Shuxun;Yu, Yizhi
We identified a novel ubiquitin-like molecule DULP from human dendritic cells. DULP contains a domain that shares 26% identity and 34% similarity with ubiquitin, and it possesses the corresponding Ile-44 hydrophobic patch used by mono- or poly-ubiquitin to interact with a ubiquitin-interaction motif (UIM) or ubiquitin-associated domain (UBA). Lysine residue corresponding to 6 of ubiquitin, which is involved in the formation of a multi-ubiquitin chain that can bind proteasomal subunit Rpn10/S5a, is also conserved in its ubiquitin-homology domain. However, DULP does not possess the highly conserved C-terminus Gly-Gly required for ubiquitin conjugation or the Lys-48 required for the formation of polyubiquitin chain to target substrates for degradation, suggesting it might be a novel ubiquitin-domain protein (UDP). DULP was found widely expressed in many cells and the ubiquitin-homology domain was not cleaved. We also confirmed that DULP expression was enriched in the nucleus and much weaker in the cytosol. Besides, we found that overexpression of DULP in 293T cells induced apoptosis, which might not be associated with the mitochondrial or proteasome pathway, with the specific mechanism remain unclear. Further investigations are needed to identify the precise biological functions of DULP. Cellular & Molecular Immunology. 2009;6(1):27-33.