An initial biochemical and cell biological characterization of the mammalian homologue of a central plant developmental switch, COP1

BMC Cell Biology

Xing Wang Deng¹  Ning Wei¹  Haiyang Wang¹  Chunling Yi¹ 

[1] Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8104, USA

关键词: RING finger;    nuclear export signal (NES);    nuclear localization/import signal (NLS);    ubiquitination;    Mammalian COP1;   

Others  :  1088939
DOI  :  10.1186/1471-2121-3-30

 received in 2002-09-11, accepted in 2002-12-04,  发布年份 2002

【 摘 要 】

Background

Constitutive photomorphogenic 1 (COP1) has been defined as a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. Although COP1 mammalian homologue has been previously reported, its function and distribution in animal kingdom are not known.

Results

Here we report the characterization of full-length human and mouse COP1 cDNAs and the genomic structures of the COP1 genes from several different species. Mammalian COP1 protein binds to ubiquitinated proteins in vivo and is itself ubiquitinated. Furthermore, mammalian COP1 is predominately nuclear localized and exists primarily as a complex of over 700 kDa. Through mutagenesis studies, we have defined a leucine-rich nuclear export signal (NES) within the coiled-coil domain of mammalian COP1 and a nuclear localization signal (NLS), which is composed of two clusters of positive-charged amino acids, bridged by the RING finger. Disruption of the RING finger structure abolishes the nuclear import, while deletion of the entire RING finger restores the nuclear import.

Conclusions

Our data suggest that mammalian COP1, similar to its plant homologue, may play a role in ubiquitination. Mammalian COP1 contains a classic leucine-rich NES and a novel bipartite NLS bridged by a RING finger domain. We propose a working model in which the COP1 RING finger functions as a structural scaffold to bring two clusters of positive-charged residues within spatial proximity to mimic a bipartite NLS. Therefore, in addition to its well-characterized role in ubiquitination, the RING finger domain may also play a structural role in nuclear import.

【 授权许可】

   
2002 Yi et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.

【 图 表 】

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